Giantin, a novel conserved Golgi membrane protein, is a disulfide-linked homodimer. It was found that BFA-induced Golgi disorganization is associated with the monomerization of giantin.

The pull-down experiment was performed. The control peptide biotin-GHGTGSTGSGSMLRTLLRRRL synthesized by LifeTein was incubated with lysate and Dynabeads, as well as the lysate incubated with Dynabeads only served as a control. Dynabeads carrying MGAT1 peptide were able to pull-down giantin from the lysate of HeLa cells, however, giantin was not detected in the pull-down fraction from the lysate exposed to the Dynabeads or in combination with control peptide. It is logical to hypothesize that the MGAT1 binding domain of giantin lies within its N-terminal non-coiled-coil area.

The Dynabeads function similarly to LifeTein magnetic beads:
https://www.lifetein.com/peptide-product/amineactivated-peptide-conjugation-magnetic-beads-p-3647.html

Cells 2019, 8(12), 1631; https://doi.org/10.3390/cells8121631

Table 1 Selection of cell-penetrating peptides

(Reference: https://doi.org/10.1007/978-981-13-8747-0, Ülo Langel, CPP, Cell-Penetrating Peptides, 2019)

Name	Sequence
2	DSLKSYWYLQKFSWR (Kondo et al. 2012)
18A	DWLKAFYDKVAEKLKEAF (Datta et al. 2000)
α1H	KSKTEYYNAWAVWERNAP (Gomarasca et al. 2017)
α2H	GNGEQREMAVSRLRDCLDRQA (Gomarasca et al. 2017)
A22p	HTPGNSNKWKHLQENKKGRPRR (Shin et al. 2014)
Ac-18A-NH2	DWLKAFYDKVAEKLKEAF) (Wimley and White 2000)
aCPP	Typical sequence R9GPLGLAGE8 (Li et al 2015)
AdVpVI(33-55)	Ac-GAFSWGSLWSGIKNFGSTVKNYG (Murayama et al. 2016)
AIP6	RLRWR (Wang et al. 2011)
all-d DsC18	Glrkrlrkfrnkikek (Bergmann et al. 2017)
αgliadin(31-43)	LGQQQPFPPQQPY (Paolella et al. 2018)
Alyteserin-2a	ILGKLLSTAAGLLSNL (Conlon et al. 2013)
ANG	TFFYGGSRGKRNNFKTEEY (Demeule et al. 2008)
ApoE(141–150)	Ac-LRKLRKRLLRX-Bpg-G (Shabanpoor et al. 2017)
ApoE-derived	Ac-LRKLRKRLLR (Tailhades et al. 2017)
Arf(1-22)	MVRRFLVTLRIRRACGPPRVRV (Johansson et al. 2008)
AT1002	FCIGRL (Gopalakrishnan et al. 2009)
AT1AR(304-318)	FLGKKFKKYFLQLLK (Östlund et al. 2005)

Bac7	RRIRPRPPRLPRPRPRPLPFPRPGPRPIPRPL (Sadler et al. 2002)
BGPC7-FHV	RRRRNRTRRNRRRVR-RRFYGPV (Wongso et al. 2017)
Bim	EIWIAQELRRIGDEFNAYYARLLC (Kim et al. 2017)
BP16	KKLFKKILKKL (Soler et al. 2014)
BP100	KKLFKKILKYL (Eggenberger et al. 2009)
BPP13a	GGWPRPGPEIPP (Sciani et al. 2017)
bPrPp(1-30)	MVKSKIGSWILVLFVAMWSDVGLCKKRPKP (Magzoub et al. 2006)
BR2	RAGLQFPVGRLLRRLLR (Lim et al. 2013)
Buforin II	TRSSRAGLQFPVGRVIIRLLRK (Park et al.1998)
Buforin IIb	RAGLQFPVG[RLLR]3 (Lee et al. 2008)
C6M1	RLWRLLWRLWRRLWRLLR (Jafari et al. 2014)
C105Y	CSIPPEVKFNKPFVYLI (Rhee and Davis 2006)
CADY	GLWRALWRLLRSLWRLLWRA cycteamide (Crombez et al. 2009a)
CAR	CARSKNKDC (Toba et al. 2014)
CA-Tat	KWKLFKKYGRKKRRQRRR (Lv et al. 2017)
CB5005 M	KLKLALALALA (Zhang et al. 2016)
CDB3	REDEDEIEW (Issaeva et al. 2003)
CendR	RPARPAR (Hu et al. 2014)
cF<tR4	cyclic F<tRRRRQ (Qian et al. 2014)
CGKRK	CGKRK (Griffin et al. 2017)
CIGB-300	cyclic CWMSPRHLGTC-Tat (Perera et al. 2012)
CIGB-552	Ac-HARIKpTFRRlKWKYKGKFW (Fernandez Masso et al. 2013)
CLIP6	KVRVRVRVpPTRVRERVK (Soudah et al. 2017)
CooP	ACGLSGLGVA (Hyvonen et al. 2014)
CpMTP	ARLLWLLRGLTLGTAPRRA (Jain and Chugh 2016)
CPNT	STSGTGKMTRAQRRAAARRNRA (Qi et al. 2011)
CPP1	(KFF)3K (Patel et al. 2017)
CPP33	RLWMRWYSPRTRAYG (Lin et al. 2018)
CPP-C	PIEVCMYREP (Nakayama et al. 2011)
CPPecp	NYRWRCKNQN (Fu et al. 2017)
C-peptide	GPGLWERQAREHSERKKRRRESECKAA (Fan et al. 2016)
CRGDK	CRGDK (Zhao et al. 2018)
Crotamine	YKQCHKKGGHCFPKEKICLPPSSDFGKMDCRWRWKCCKKGSG (Rodrigues et al. 2012)
cSN50	AAVALLPAVLLALLAPVQRKRQKLMP (Torgerson et al. 1998)
65-2CTS	CPYVNQRPQKARYRNG (Percipalle et al. 2003)
CWR8K	CWR8K (Sasaki et al. 2008)
CyLoP-1	CRWRWKCCKK (Ponnappan et al. 2017)

Cyt c(77–101)	GTKMIFVGIKKKEERADLIKKA (Howl and Jones 2015)
DAG	cyclic CDAGRKQKC (Mann et al. 2017)
D-JNKI-1	RPKRPTTLNLFPQVPRSQDT (Bonny et al. 2001)
DK17	DRQIKIWFQNRRMKWKK (Bera et al. 2016)
DLP	ACKTGSHNQCG (Kumar et al. 2015)
DMBT1-derived	GRVEVLYRGSW and GRVRVLYRGSW (Tuttolomondo et al. 2017)
dNP2	KIKKVKKKGRK-KIKKVKKKGRK (Lim et al. 2015)
DPV3	RKKRRRESRKKRRRES (Tacken et al. 2008)
DPV1047	CVKRGLKLRHVRPRVTRMDV (De Coupade et al. 2005)
DRTTLTN	DRTTLTN (Gennari et al. 2016)
DS4.3	RIMRILRILKLAR (Jeong et al. 2014)
Dynorphin A	YGGFLRRIRPKLKWDNQ (Marinova et al. 2005)
EA	GLKKLAELAHKLLKLGC (Yang et al. 2014)
EB1	LIRLWSHLIHIWFQNRRLKWKKK (Lundberg et al. 2007)
EF	GLKKLAELFHKLLKLGC (Yang et al. 2014)
EHB	RCSHYTGIRCSHMAATTAGIYTGIRCQHVVL-C6H (Cao et al. 2018)
EPRNEEK	EPRNEEK (Orihuela et al. 2009)
F3**	diphosphorylated dipeptide (Miao et al. 2016)
G4R9L4	G4R9L4 (Ramakrishna et al. 2014)
GALA	WEAALAEALAEALAEHLAEALAEALEALAA (Li et al. 2004)
GeT	KIAKLKAKIQKLKQKIAKLK (Rakowska et al. 2014)
gH625	HGLASTLTRWAHYNALIRAF (Galdiero et al. 2015)
Gi3α(346-355)	KNNLKECGLY (Jones et al. 2005)
Glu-Lys	EEEAAKKK (Lewis et al. 2010)
GV1001	EARPALLTSRLRFIPK (Kim et al. 2016a)
GWH1	GYNYAKKLANLAKKFANALW (Serna et al. 2017)
H2A derived	SGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKG (Rosenbluh et al. 2004)
H6R6	H6R6 (Sun et al. 2017)
H16	H16 (Iwasaki et al. 2015)
HA2(1-23)	GLFGAIAGFIENGWEGMIDGWYG (Esbjörner et al. 2007)
HAIYPRH	HAIYPRH (Shteinfer-Kuzmine et al. 2017)
hBD3-3	GKCSTRGRKCCRRKK (Lee et al. 2015b)
HBP	GKRKKKGKGLGKKRDPCLRKYK (Luo et al. 2016)
hLF	KCFQWQRNMRKVRGPPVSCIKR (Duchardt et al. 2009)
Hph-1	YARVRRRGPRR (Jung et al. 2011)
HR9	CH5-R9-H5C (Liu et al. 2013a)

Hst5	DSHAKRHHGYKRKFHEKHHSHRGY (Luque-Ortega et al. 2008)
I1WL5W	WKKIWSKIKKLLK (Bi et al. 2014)
I4WL5W	IKKWWSKIKKLLK (Bi et al. 2014)
ID No.2	MAAWMRSLFSPLKKLWIRMH (Eudes and Macmillan 2014)
IMT-P8	RRWRRWNRFNRRRCR (Gautam et al. 2016)
INF	GLFEAIEGFIENGWEGMIDGWYGC (Pichon et al. 1997)
iNGR	CRNGRGPDC (Alberici et al. 2013)
isl-1	RVIRVWFQNKRCKDKK (Kilk et al. 2001)
JB9	cskc (Basu and Wickstrom, 1997)
JB434	R9GGLAA-Aib-SGWKH6 (Sangtani et al. 2018)
KAFAK	KAFAKLAARLYRKALARQLGVAA (Bartlett et al. 2013)
KALA	WEAKLAKALAKALAKHLAKALAKALKACEA (Wyman et al. 1997)
Kalata B1	polycyclic CGETCVGGTCNTPGCTCSWPVCTRNGLPV (Daly et al. 1999)
(KFF)3K	(KFF)3K (Rownicki et al. 2017)
K-FGF	AAVLLPVLLAAP (Lin et al. 1995)
KH	(KH)9 (Chuah et al. 2016)
KLA	KLAKLAKKLAKLAK (Huang et al. 2017)
KLAK	KLALKLALKALKAALKLA (Oehlke et al. 1998)
KLA-R7	KLAKLAKKLAKLAKGGRRRRRRR (Lemeshko, 2013)
KP	MAPTKRKGSCPGAAPNKKP (Villa-Cedillo et al. 2017)
KST peptide	STGKANKITITNDKGRLSK (Adachi et al. 2017)
L1−6	PLILLRLLR (Schmidt et al. 2017)
L5a	RRWQW (Liu et al. 2016a)
L17E	IWLTALKFLGKHAAKHEAKQQLSKL (Akishiba et al. 2017)
lactoferrampin(265- 284)	DLIWKLLSKAQEKFGKNKSR (Reyes-Cortes et al. 2017)
lactoferricin(17-30)	FKCRRWQWRMKKLG (Reyes-Cortes et al. 2017)
lactoferrin(19-40)	KCFMWQEMLNKAGVPKLRCARK (Duchardt et al. 2009)
LAH1	KKLALALALALHALALALALKKA (Moulay et al. 2017)
LALF(31-52)	HYRIKPTFRRLKWKYKGKFW (Yanez et al. 2017)
LB	FKCRRWQWRMKKLGAPSITCVRRAF) (Liu et al. 2013b)
L-CPP	LAGRRRRRRRRRK (Liu et al. 2006)
LDP-NLS	KWRRKLKKLRPKKKRKV (Ponnappan and Chugh, 2017)
LE10	LELELELELELELELELELE (Antunes et al. 2013)
LF chimera	FKCRRWQWRMKKLG-K-RSKNKGFKEQAKSLLKWILD (Reyes-Cortes et al. 2017)

linTT1	AKRGARSTA (Hunt et al. 2017)
LK	LKKLLKLLKKLLKLAG (Kim et al. 2016b)
LL37	LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES (Kim et al. 2016b)
LLIIL	LLIIL (Alaybeyoglu et al. 2017)
LMWP	VSRRRRRRGGRRRR (Chen et al. 2017d)
LP-12	HIITDPNMAEYL (Kumar et al. 2015)
LPAs	RCnRCnK (Gupta et al. 2011)
LTV	LTVSPWY (Chopra 2012)
lycosin-I	RKGWFKAMKSIAKFIAKEKLKEHL (Tan et al. 2017)
Lyp1	CGNKRTRGC (Fogal et al. 2008)
M918	MVTVLFRRLRIRRACGPPRVRV (El-Andaloussi et al. 2007)
Maurocalcine	GDCLPHLKLCKENKGCCSKKCKRRGTNIEKRCR (Poillot et al. 2010)
MAP	KLALKLALKALKAALKLA (Oehlke et al. 1998)
MAP12	LKTLTETLKELTKTLTEL (Oehlke et al. 2002)
MCoTI-I	polycyclic SGSDGGVCPKILQRCRRDSDCPGACICRGNGYCG (Camarero, 2017)
MCoTI-II	polycyclic CPKILKKCRRDSDCPGACICRGNGYCGSGSDGGV (Huang et al. 2015)
MFK	MFKLRAKIKVRLRAKIKL (Samuels et al. 2017)
Mgpe9	CRRLRHLRHHYRRRWHRFRC (Vij et al. 2016a)
MitP	INLKKLAKL(Aib)KKIL (Howl et al. 2018)
m(KLA)-iRGD	klaklakklakla-K-GG-iRGD (Qifan et al. 2016)
MMGP1	MLWSASMRIFASAFSTRGLGTRMLMYCSLPSRCWRK (Pushpanathan et al. 2013)
MPER fragment	ELDKWASLWNWFDITNWLWYIK (Song et al. 2009)
MPG	GALFLGFLGAAGSTMGA cysteamide (Morris et al. 1997)
MPG	GALFLGFLGAAGSTMGASQPKKKRKV cycteamide (Deshayes et al. 2005)
MPG-8	AFLGWLGAWGTMGWSPKKKRK (Crombez et al. 2009b)
mRVG	YTIWMPENPRPGTPCDIFTKSRGKRASNGGGRRRRRRRRR (Villa-Cedillo et al. 2017)
MT23	LPKQKRRQRRRM (Zhou et al. 2017)
mtCPP1	r-Dmt-OF (Cerrato et al. 2015)
MTM	AAVALLPAVLLALLAP (Fletcher et al. 2010)
MTD84	AVALVAVVAVA (Lim et al. 2014)
MTP	MLSLRQSIRFFK (Chuah et al. 2015a, b)
MTS	KGEGAAVLLPVLLAAPG (Zhao et al. 2001)
MTS1	AAVLLPVLLAAP (Rojas et al. 1998)
Mut3DPT-C9h	VKKKKIKAEIKIYVETLDDIFEQWAHSEDL (de la Torre et al. 2017)

Myr-ApoE	Myr-LRKLRKRLLR (Tajik-Ahmadabad et al. 2017)
New modalities	Polycyclic, hairpin, stapled peptides for delivery (Valeur et al. 2017, Waldmann et al. 2017)
NF1	Stearyl-AGY(PO3)LLGKTNLKALAALAKKIL (Arukuusk et al. 2013)
NF51	δ-(Stearyl-AGYLLG)OINLKALAALAKKIL (Arukuusk et al. 2013)
NF55	δ-(Stearyl-AGYLLG)OINLKALAALAKAIL (Freimann et al. 2016)
NLS	PKKKRKV (Yoneda et al. 1992).
NLS-StAx-h	stapled RRWPRXILDXHVRRVWR (Dietrich et al. 2017)
NoLS	KKRTLRKNDRKKRC (Yao et al. 2015)
Novicidin	KNLRRIIRKGIHIIKKYF (Milosavljevic et al. 2016)
NPFSD	VLTNENPFSDP (Gong et al. 2016)
NYAD-1	stapled ITFEDLLDYYGP (Zhang et al. 2008)
Oct4-PTD	DVVRVWFCNRRQKGKR (Adachi et al. 2017)
P007	Ac-(RAhxR)4-Ahx-βAla (Greer et al. 2014)
P1	LRRWSLG (Peng et al. 2017b)
P2	WKRTLRRL (Peng et al. 2017b)
P3	YGRKKRRQR (Tan et al. 2006)
P7	RRMKWKK (Watson et al. 2017)
P11	YGRKKRRQRRR (Zhao et al. 2011)
P11	HSDVHK (Bang et al. 2011)
P11LRR	P11LRR (Li et al. 2010)
P14LRR	(PLPRPR)4 (Brezden et al. 2016)
p18	LSTAADMQGVVTDGMASG (Taylor et al. 2009)
P21	KRKKKGKGLGKKRDPCLRKYK (Dixon et al. 2016)
P28	LSTAADMQGVVTDGMASGLDKDYLKPDD, Leu50-Asp77 of azurin (Yamada et al. 2016)
p28	FLHSGTAVTCTYPALTPQWEGSDCTHRL (Signorelli et al. 2017)
p53 peptide MO6	Stapled TSF*EYWYLL* (Chee et al. 2014)
PAF26	Ac-rkkwfw (Lopez-Garcia et al. 2002)
PAS	GKPILFF (Woldetsadik et al. 2017)
pCLIP6	KVRVRVRVpP(pT)RVRERVK (Chen et al. 2017b)
pD-SP5	riPRPSPKMGV(pS)VS (Chen et al. 2017b)
PenetraMax	KWFKIQMQIRRWKNKR, L- and D- (Khafagy el et al. 2015)
Penetratin	RQIKIWFQNRRMKWKK (Derossi et al. 1994)
Pep-1	KETWWETWWTEWSQPKKKRKV cysteamide (Morris et al. 1997)
pepM	KLFMALVAFLRFLTIPPTAGILKRWGTI (Freire et al. 2014)
pepR	LKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRR (Freire et al. 2014)
Pept1	PLILLRLLRGQF (Marks et al. 2011)

Peptide 599	GLFEAIEGFIENGWEGMIDGWYGGGGRRRRRRRRRK (Alexander-Bryant et al. 2015)
Pep42	Cyclic CTVALPGGYVRVC (Kim et al. 2006)
PepNeg	SGTQEEY (Neves-Coelho et al. 2017)
PepFect6	Stearyl-AGYLLGK(εTMQ)INLKALAALAKKIL, PF6 (El-Andaloussi et al. 2011)
PepFect14	Stearyl- AGYLLGKLLOOLAAAALOOLL (Ezzat et al. 2011)
PG1	RGGRLCYCRRRFCVCVGR (Liu et al. 2013b)
pHLIP	AEQNPIY-WARYADWLFTTPLLLLDLALLV-DADEGT (Andreev et al. 2010)
PHPs	H6-H10 peptides (Kimura et al. 2017)
PIP1	RXRRXRRXRIKILFQNRRMKWKK (Ivanova et al. 2008)
Pip5e	RXRRBRRXRILFQYRXRBRXRB (Betts et al. 2012)
Pip6a	Ac-RXRRBRRXRYQFLIRXRBRXRB (Lehto et al. 2014)
POD	CGGG(ARKKAAKA)4 (Dasari et al. 2017)
PR9	FFLIPKG-R9 (Liu et al. 2013a)
PTD	YARVRRRGPRRR (Dong et al. 2016)
PTD3	R9-ETWWETWWTEW (Kizaka-Kondoh et al. 2009)
PTD4	YARAAARQARA (McCusker et al. 2007)
Poly-Arg	Most popular R7 – R12 (Mitchell et al. 2000, Futaki, 2006)
pVEC	LLIILRRRIRKQAHAHSK (Elmquist et al. 2001)
Pyrrhocoricin	VDKGSYLPRPTPPRPIYNRN (Otvos et al. 2000)
R4K1	Stapled Ac-RRRRKS*LHRS*LQDS (Speltz et al. 2018)
R6dGR	R6dGR (Wang et al. 2017)
R8	R8 (Wender et al. 2001)
R8-dGR	R8dGR (Liu et al. 2016b)
R9-H4A2	Ac-YR9-HAHAHH (Okitsu et al. 2017)
R6W3	R6W3 (Bechara et al. 2013)
R10W6	R10W6 (Bechara et al. 2013)
RA9	RRAARRARR (Alhakamy et al. 2013)
RALA	WEARLARALARALARHLARALARALRACEA (McCarthy et al. 2014)
RDP	CKSVRTWNEI IPSKGCLRVG GRCHPHVNGG GRRRRRRRRC (Xiao et al. 2017)
REDV	REDV (Yang et al. 2016)

RF	GLKKLARLFHKLLKLGC (Yang et al. 2014)
cRGDfC	Cyclic RGDfC (Wada et al. 2017)
iRGD	Cyclic CRGDKGPDC (Peng and Kopecek, 2015)
RGE	RGERPPR (Yu et al. 2017)
RH9	RRHHRRHRR (Alhakamy et al. 2013)
RL9	RRLLRRLRR (Alhakamy et al. 2013)
RL16	RRLRRLLRRLLRRLRR (Joanne et al. 2009)
RT53	RQIKIWFQNRRMKWKKAKLNAEKLKDFKIRLQYFARGLQV YIRQLRLALQGKT (Jagot-Lacoussiere et al. 2016)
RTP004	RKKRRQRRRG-K15-GRKKRRQRRR) (Lee et al. 2015a)
RV24	RRRRRRRRRGPGVTWTPQAWFQWV (Lo and Wang, 2012)
RVG	YTIWMPENPRPGTPCDIFTNSRGKRASNG (Kumar et al. 2007)
RVG-9R	YTIWMPENPRPGTPCDIFTNSRGKRASNGGGGRRRRRRRRR (Rassu et al. 2017)
RVG29	YTIWMPENPRPGTPCDIFTNSRGKRASNGGGGRRRRRRRRR (Villa-Cedillo et al. 2017)
RW9	RRWWRRWRR (Alhakamy et al. 2013)
RW16	RRWRRWWRRWWRRWRR (Jobin et al. 2013)
(RXR)4	(R-Ahx-R)4 (Saleh et al. 2010)
(rXr)4	(r-Ahx-r)4 (Vij et al. 2016b)
S155	VKKKKIKREI-KIAAQRYGRELRRMADEFHV (Haidar et al. 2017)
S4(13)-PV	ALWKTLLKKVLKAPKKKRKV (Mano et al. 2007)
SAP	VRLPPPVRLPPPVRLPPP (Pujals et al. 2006)
SAP(E)	VELPPPVELPPPVELPPP (Martin et al. 2011)
all-D-SAP	(vrlppp)3 (Pujals et al. 2007)
SAPSp-lipo	stearyl-GGGGHGAHEHAGHEHAAGEHHAHE (Suzuki et al. 2017)
SAR6EW	SAR6EW (Im et al. 2017)
sC18	GLRKRLRKFRNKIKEK (Oren et al. 1999)
(sC18)2	(GLRKRLRKFRNKIKEK)2 (Gronewold et al. 2017)
SMTP motif,	LRLLR (Fuselier and Wimley, 2017)
SPACE	Cyclic ACTGSTQHQCG (Hsu and Mitragotri, 2011)
SRCRP2-11	GRVEVLYRGSW (Tuttolomondo et al. 2017)
STR-KV	H3K3V6 (Pan et al. 2016)
SS-02	Dmt-r-FK (Alta et al. 2017)
SS-20	F-r-FK (Alta et al. 2017)
SS-31	r-Dmt-KF (Zhao et al. 2005)
SynB1	RGGRLSYSRRRFSTSTGR (Rousselle et al. 2000)
T2	LVGVFH (Kumar et al. 2012)

Tat(49-57)	RKKRRQRRR (Vives et al. 1997a)
Tat(48-60)	GRKKRRQRRRPPQ (Vives et al. 1997b)
Tat(44-57)	CGISYGRKKRRQRRR (Niesner et al. 2002)
Tat(37-72)	CFITKALGISYGRKKRRQRRRPPQGSQT-HQVSLSKQ (Fawell et al. 1994)
Tat analog	GRKKRRQR (Nguyen et al. 2008)
Tat-LK15	Tat-KLLKLLLKLLLKLLK (Peng et al. 2017a)
TCTP	MIIFRALISHKK (Bae et al. 2016)
TD-1	ACSSSPSKHCG (Chen et al. 2006)
TD2.2	SYWYRIVLSRTGRNGRLRVGRERPVLGESP (Heffernan et al. 2012)
TH peptide	GYLLGHINLHHLAHL-Aib-HHIL (Chen et al. 2017a)
TM2	PKKGSKKAVTKAQKKDGA (Kochurani et al. 2015)
Transportan	GWTLNSAGYLLGKINLKALAALAKKIL, TP (Pooga et al. 1998)
TP10	AGYLLGKINLKALAALAKKIL (Soomets et al. 2000)
TPk	VRRFkWWWkFLRR (Bahnsen et al. 2015)
Tpl	KWCFRVCYRGICYRRCRGK (Jain et al. 2015)
TPP	TKDNNLLGRFELSG (Gehrmann et al. 2014)
TT1	CKRGARSTA (Paasonen et al. 2016)
vAMP 059	INWKKWWQVFYTVV (Dias et al. 2017)
vCPP 0769	RRLTLRQLLGLGSRRRRRSR (Dias et al. 2017)
vCPP 2319	WRRRYRRWRRRRRWRRRPRR (Dias et al. 2017)
VDAC(1-26)	MAVPPTYADLGKSARDVFTKGYGFGL (Smilansky et al. 2015)
VP22	NAATATRGRSAASRPTQRPRAPARSASRPRRPVQ (Elliott and O’Hare, 1997)
V peptide	TVDNPASTTNKDKLFAVRK (Manosroi et al. 2014)
VT5	DPKGDPKGVTVTVTVTVTGKGDPKPD (Oehlke et al. 1997)
W(RW)4	W(RW)4 (Nasrolahi Shirazi et al. 2013)
Xentry	LCLR (Montrose et al. 2014)
X-pep	MAARLC (Adachi et al. 2017)
YKA	YKALRISRKLAK (Desai et al. 2014)
YTA2	YTAIAWVKAFIRKLRK (Lindgren et al. 2006)
YTA4	IAWVKAFIRKLRKGPLG (Lindgren et al. 2006)
Z2	FWIGGFIKKLKRSKLA (Chen et al. 2017c)
Z3	FKIKKFIGGLWRSKLA (Chen et al. 2017c)
Z12	KRYKNRVASRKCRAKFKQLLQHYREVAAAKSSENDRLRLLLK (Derouazi et al. 2015)
ZXR-1	FKIGGFIKKLWRSKLA (Chen et al. 2017c)

[/showhide]

LifeTein provides the fastest turnaround time and most reliable quality in the industry. Peptides are made in New Jersey, USA. Projects move from conception to bench in only 3–5 days so you can deal with your research deadlines.

Introducing LifeTein‘s faster microwave peptide synthesis technology!
LifeTein’s new platform is designed for maximized speed and efficiency. Unparalleled peptide quality, greater flexibility, and improved reliability make LifeTein the vendor of choice for all your peptide synthesis needs.

Remarkably Fast:

• Rush synthesis service in 3-5 Days
• Difficult peptides such as beta-Amyloid in hours rather than days
• 4-minute cycle time

Aβ-(1–42) was dissolved to 1 mM in 100% hexafluoroisopropanol, hexafluoroisopropanol was removed under vacuum, and the peptide was stored at −20 °C. For the aggregation protocols, the peptide was first resuspended in dry Me2SO (DMSO) to 5 mM. For oligomeric conditions, F-12 (without phenol red) culture media was added to bring the peptide to a final concentration of 100 μM, and the peptide was incubated at 4 °C for 24 h. For fibrillar conditions, 10 mM HCl was added to bring the peptide to a final concentration of 100 μM, and the peptide was incubated for 24 h at 37 °C.

ADDLS, amyloid-derived diffusible ligands.

Preparing human islet amyloid polypeptide (hIAPP), also known as amylin, can be challenging due to its hydrophobic amino acid residues.

Here’s an improved method for dissolving lyophilized hIAPP:

1. Begin by dissolving lyophilized hIAPP in 80% (v/v) HFIP containing 10 mM HCl. This step ensures complete dissolution. The CD spectrum indicates the presence of a stable alpha-helical conformation, which remains so for several days.
2. Next, remove the HFIP by lyophilization, leaving behind lyophilized hIAPP.
3. Re-dissolve the lyophilized hIAPP in 10 mM HCl, and eliminate any insoluble components by ultracentrifugation.
4. The resulting hIAPP solution in 10 mM HCl is ready for immediate use in experiments.

To initiate the formation of hIAPP fibrils, introduce the stock solution into the reaction buffer. Conditions for fibril formation were optimized under two pH conditions:

• Low pH: Utilize 25 uM hIAPP in 10 mM HCl, with varying concentrations of HFIP.
• Neutral pH: Employ 25 uM hIAPP in a 50 mM sodium phosphate buffer at pH 7.0, with varying concentrations of HFIP.

Incubate these samples at 25 °C for several hours.

Reference: JOURNAL OF BIOLOGICAL CHEMISTRY 23965, JULY 8, 2011 VOLUME 286 NUMBER 27

Aducanumab is a human monoclonal antibody that has been studied for the treatment of Alzheimer’s disease.

LifeTein Synthesized a Key Peptide That Played a Role in the Nobel Prize in Physiology or Medicine 2019

The Nobel Prize in Physiology or Medicine 2019 was awarded jointly to William G. Kaelin Jr., Sir Peter J. Ratcliffe, and Gregg L. Semenza. LifeTein made one of the key peptides: HIF1a-P564: DLDLEMLAPYIPMDDDFQLR.

A click chemistry was reported about the formation of azides from primary amines. This powerful tool enables the reaction of just one equivalent of a simple diazotizing species, and fluorosulfuryl azide (FSO2N3), for the preparation of over 1,200 azides on 96-well plates in a safe and practical manner. This method greatly expands the number of accessible azides and 1,2,3-triazoles because the primary amine is one of the most abundant functional groups in small compounds, proteins and antibodies.

Formation of Azides From Primary Amines

The method opens the door for numerous applications in drug screening and discovery. The cell penetration peptides can be easily introduced to conjugate with any azide containing drugs, compounds, antibodies, or proteins.

The cell penetration peptides (CPPs) are capable of delivering biologically active cargo to the cell interior. The desired therapeutic cargo could be attached to a CPP using the copper free click chemistry and then delivered to an intracellular target, thereby overcoming the entry restrictions set by the plasma membrane.

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LifeTein Synthesized a Key Peptide That Played a Role in the Nobel Prize in Physiology or Medicine 2019

BRAF is an RAF kinase. It is a core component of the RAS/RAF/MEK/ERK signaling cascade, known as mitogen-activated protein kinase (MAPK) pathway. It is one of the major effectors of oncogene RAS, and is often mutated in human cancer cells.

LifeTein’s Braftide & Cancer Therapy

Two FDA approved drugs, Dabrafenib, and vemurafenib, effectively inhibit the most common BRAF variant V600E, a monomeric BRAF. But, the non-V600E BRAF mutations are intrinsically resistant to these drugs. These drugs may also paradoxically stimulate the pathway when the tumor cells contain wild-type BRAF and oncogenic RAS, causing secondary malignancies.
The researchers tried to tackle the dimeric BRAF. The dimeric BRAF, such as the wild type and G469A, a most prevalent non-V600E variant in lung cancer cells, hinges on dimer interface (DIF), a 20aa span near the tail end of the alpha-C helix of BRAF. The researchers designed Braftide using computational modeling, aiming to block the dimerization. They tested the functionality in vitro, in HEK263 cells and colon cancer cell lines.

LifeTein synthesized Braftide (TRHVNILLFM), Null-Braftide (THHVNILLFM), Cy3-Braftide (TRHVNILLFM-Cy3), TAT-Braftide (GRKKRRQRRRPQ-PEG-TRHVNILLFM), and TAT (GRKKRRQRRRPQ). We reviewed here some of the assays that helped support Braftide as an allosteric inhibitor of BRAF dimer and down-regulator of MAPK signaling pathway for cancer therapy.

1) Cell-free in vitro assay: dose-response curve. First of all, the researchers show that Braftide has a sub-micromolar IC50 for dimeric BRAF. Full-length dimeric BRAF-WT and BRAF-G469A (from HEK293F cells) were used for dose-response curves, and the BRAF activity was probed by pMEK production.

2) Cell-free in vitro assay: Saturation binding assay. The researchers used Cy3-labeled Braftide (Cy3-Braftide) to characterize (KD) the binding of Braftide with dimeric BRAF-WT using fluorescence quantification.

3) Cell-free in vitro assay: Immunoprecipitation (IP). The purpose of IP was to show Braftide disrupted the BRAF dimerization. Braftide was added to HEK293 cell lysate coexpressing V5- and FLAG-tagged BRAF-WT. FLAG-tagged BRAF was pulled down by FLAG antibody-conjugated resin, which was further probed for V5-tagged BRAF. Braftide indeed reduced homodimer BRAF.

4) Delivery of Braftide into HEK cell for BRAF inhibition. Braftide was tagged with cell-penetrating peptide TAT. TAT-Braftide (and its negative control TAT alone) was used to treat HEK293 cells transiently transfected with BRAF-WT and BRAF-G469A. Four hours of treatment resulted in reductions of BRAF, pMEK, MEK (i.e. the MAPK pathway), which were analyzed with respective antibodies by immunoblotting.

5) Delivery of Braftide into cancer cells for BRAF inhibition and cell proliferation inhibition. Two colon cancer cell lines (KRAS-G13D-colon carcinoma) were treated with cell-penetrating TAT-Braftide and assayed for the inhibition of BRAF activity, down-regulation of MAPK signaling, and cell proliferation. All were shown positive, while the negative control TAT alone were negative.

https://pubs.acs.org/doi/abs/10.1021/acschembio.9b00191

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Synthetic Scorpion Toxin Peptides for Chronic Pain

Researchers at the University of California, San Francisco (UCSF), in collaboration with LifeTein, have made a groundbreaking discovery in the field of pain management. LifeTein’s expertise in peptide synthesis was crucial in developing synthetic scorpion toxin peptides that specifically target the “wasabi receptor,” a key player in the body’s response to certain types of pain.

The wasabi receptor, scientifically known as TRPA1, is an ion channel protein that triggers the familiar sinus-clearing or eye-watering sensation experienced when consuming wasabi or cutting onions. This receptor is also implicated in the perception of chronic pain.

The focus of this research is a peptide derived from scorpion toxin, referred to as WaTx. Remarkably, WaTx, synthesized by LifeTein, can activate the TRPA1 receptor, mimicking the pain response to irritants. Unlike other molecules, WaTx has the unique ability to penetrate cell membranes directly, bypassing the need for channel proteins. This property makes it an invaluable tool for studying chronic pain and inflammation.

In addition to its research applications, WaTx holds promise for the development of new, non-opioid pain therapies. It has been observed to induce pain and pain hypersensitivity without causing neurogenic inflammation, a common side effect of many pain treatments.

Expanding the Horizon: Spider Venom and Chronic Pain

Further expanding on this concept, a study titled “Identification and Characterization of ProTx-III [μ-TRTX-Tp1a], a New Voltage-Gated Sodium Channel Inhibitor from Venom of the Tarantula Thrixopelma pruriens” delves into the potential of spider venoms in pain management. This study, conducted by F. C. Cardoso and colleagues, discovered a novel inhibitor, μ-TRTX-Tp1a (Tp1a), from the venom of the Peruvian green-velvet tarantula. Tp1a selectively inhibits human NaV1.

7 channels, which are key contributors to pain perception.

The study found that Tp1a, both in its recombinant and synthetic forms, preferentially targets NaV1.7 channels, offering a new avenue for analgesic drug development. Unlike many other spider toxins affecting NaV channels, Tp1a does not significantly alter the voltage dependence of activation or inactivation of these channels. This unique feature of Tp1a was demonstrated to be effective in reversing spontaneous pain in animal models.

The structural analysis of Tp1a revealed an inhibitor cystine knot motif, common in spider toxins but with distinct pharmacological properties that could be crucial in developing more selective and potent treatments for chronic pain.

Conclusion

The research at UCSF, along with the findings on spider venom peptides and the significant contributions of LifeTein in peptide synthesis, represents a significant step forward in understanding and potentially treating chronic pain. These discoveries highlight the vast potential of natural toxins in medical research, offering hope for more effective and safer pain management strategies in the future.

Reference:

• Lin King, J. V., Emrick, J. J., Kelly, M. J. S., Herzig, V., King, G. F., Medzihradszky, K. F., & Julius, D. (2019). A Cell-Penetrating Scorpion Toxin Enables Mode-Specific Modulation of TRPA1 and Pain. Cell. doi:10.1016/j.cell.2019.07.014

In humans, liver-derived insulin-like growth factor (IGF1) drives postnatal growth. Early childhood infection of E. coli, Campylobacter spp., even asymptomatic, reduces IGF1 level and restricts early-childhood growth. Does the pathogen-induced Toll-like innate immune signaling contribute to growth restriction? To answer the question, the researchers examined a corresponding pathway in fruit flies.

LifeTein’s Peptide: FLAG(GS)HA

In fruit flies, Dilps (Drosophila insulin-like peptides) drive their growth, for example, the growth rate of imaginal discs which give rise to adult structures such as wings. Dilps share homology with insulin and IGF1, and they bind to the insulin receptor. Dilp6 is produced by fat body, an organ for nutrient storage and immune functions.

The researchers found Dilp6 is a selective target of Toll signaling in the fat body, an innate immune response from bacterial infections. They also found that Toll signaling reduces Dilp6 transcripts, and dramatically suppresses circulatory Dilp6 levels, and restricts whole-body growth. Restoring Dilp6, on the other hand, rescues growth and viability in fruit flies even with active Toll signaling.

LifeTein’s peptide FLAG(GS)HA was used as a standard in ELISA to quantify Dilp6 in fruit fly hemolymph samples. Here, Dilp6 was tagged with FLAG and HA because of FLAG- and HA-tagged Dilp6HF allele from CRISPR/CAS9. In this ELISA assay, the plate wells were coated with anti-FLAG antibody, then FLAG(GS)HA or fruit fly hemolymph sample were added to the wells. FLAG(GS)HA and FLAG- and HA-tagged Dilp6 were quantified by anti-HA-Peroxidase 3F10 antibody and subsequent chromogenic reaction. For more details of the method, see the section “Hemolymph Dilp6 measurements by ELISA” in the link.

https://www.sciencedirect.com/science/article/pii/S2211124719309052

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LifeTein’s Braftide & Cancer Therapy

Peptide amphiphiles are composed of hydrophobic alkyl tails and peptide regions designed to self-assemble into cylindrical supramolecular nanofibers in solution. While hydrogen bonds form some β-sheets between short β-strands (2 or 3 residues), others are formed by extended-strands.

Smaller Ions Stabilize β-sheets

The strongly-hydrated ions (F- and Cl-) are more attracted to the positively charged lysine residues on the surface of the peptide nanofiber. When peptide residues form β-sheets, an F- or Cl- ion forms a salt bridge between the side chains of lysine residues from two neighboring peptide amphiphile chains. The salt bridge stabilizes the peptide by bringing the backbones closer, resulting in a transition from random coil to extended β-sheets structures. The smaller ions (F- and Cl-, 50mM NaF and NaCl solutions) tend to stabilize β-sheets slightly better compared to the larger ions (I-, Br-).

So, the self-assembly of peptide amphiphiles into supramolecular nanofibers can be regulated by modifying the salt solution.

Reference: doi.org/10.1021/acs.jpcb.9b05532