LifeTein can help in your research with custom peptide synthesis of the following specific proteins: SARS-CoV-2 Receptor Binding Domains, SARS-CoV-2 Nucleocapsid Fragments, T-cell and B-cell Epitopes of SARS-CoV-2, Fusion Inhibitors Targeting HR1 Domain of the SARS-CoV-2 Spike Proteins, Inhibitors of SARS-CoV-2 Mpro/3CLpro/C30 Endopeptidase, ACE2 Inhibitors and Substrates, and AT2 Receptor Agonists and Antagonists.

Pool of 22 peptides derived from a peptide design (15mers with 5 aa overlap) through the receptor binding domain of S1 protein.

Modifications: N-Terminal: Biotin Labeling

Amount: 1mg per peptide

Purity: 95%

Delivery Format: Freeze dried powder

Application(s): Antibody screening, T-cell assays, Immune monitoring, Antigen specific T-cell stimulation, Cellular immune response

Indication(s)/Topic(s): Covid-19, Infection, Respiratory infection

Delivery Time: 2 weeks

SARS-CoV-2 Receptor Binding Domains Overlapping Peptide Pools:

• QPTESIVRFPNITNL
• NITNLCPFGEVFNAT
• VFNATRFASVYAWNR
• YAWNRKRISNCVADY
• CVADYSVLYNSASFS
• SASFSTFKCYGVSPT
• GVSPTKLNDLCFTNV
• CFTNVYADSFVIRGD
• VIRGDEVRQIAPGQT
• APGQTGKIADYNYKL
• YNYKLPDDFTGCVIA
• GCVIAWNSNNLDSKV
• LDSKVGGNYNYLYRL
• YLYRLFRKSNLKPFE
• LKPFERDISTEIYQA
• EIYQAGSTPCNGVEG
• NGVEGFNCYFPLQSY
• PLQSYGFQPTNGVGY
• NGVGYQPYRVVVLSF
• VVLSFELLHAPATVC
• PATVCGPKKSTNLVK
• TNLVKNKCVNFNFNG

The cationic host defense peptides (CHDP), also known as antimicrobial peptides, could be used to kill enveloped viruses such as the 2019 Novel Coronavirus SARS-CoV-2. The peptides have the potential to destabilize the viral envelope on contact, damaging the virions and inhibiting infectivity. The specific antiviral peptide may bind to cellular receptors involved in viral infection or peptide-mediated aggregation of viral particles. The antiviral peptides could create an ‘antiviral shield’ at mucosal surfaces and prevent replication and spread of the Coronavirus if upregulated after the initial infection.

During pandemics, where there is insufficient time to produce vaccines (such as the outbreak of respiratory illness Covid-19 first detected in Wuhan, China), the cationic host defense peptides could be the first-line antiviral treatments.

Some of the antimicrobial peptides are the human cathelicidin LL-37 and β-defensins. Cathelicidins are immunomodulatory antimicrobials with an important role in the regulation of the inflammatory response. The only human cathelicidin, LL-37, is the most well-studied peptide in this family. LL-37 is an α-helical peptide. While defensins have a common β-sheet core stabilized with three disulfide bridges between six conserved cysteine residues.

Direct antimicrobial mechanisms of cationic host defense peptides can be mediated by membrane translocation of the peptides followed by binding to intracellular targets such as nucleic acids and/or proteins to kill bacteria. Proline-rich antimicrobial peptides use inner membrane transporters as Trojan horses to gain entry and bind to intracellular targets such as nucleic acids or nascent proteins. And subsequently affect cell processes such as replication, transcription, translation, protein folding, and cell wall synthesis.

At this stage, only a few peptide-derived treatments have made it to market such as PAC-113, a histatin analog, and dalbavancin, a semisynthetic lipoglycopeptide.

Despite the limited understanding of structure-function relationships, the potential of peptide-based therapies remains a promising new clinical direction for the Coronavirus.

The extensive structural analyses have revealed that interactions between SARS-CoV spike protein receptor-binding domain (RBD) and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of SARS-CoV.

Studies showed that the sequence of 2019-nCoV coronavirus RBD, including its receptor -binding motif (RBM) that directly contacts ACE2 and uses ACE2 as its receptor with much higher affinity (10-20 times higher!) than SARS.

Several critical residues in 2019-nCoV RBM may provide favorable interactions with human ACE2 such as Gln493 and Asn501.

A total of nine cysteine residues are found in the RBD, six of which forming three pairs of disulfide bonds. Among these three pairs, two are in the core (Cys336-Cys361 and Cys379-Cys432) to help stabilize the β sheet structure while the remaining one (Cys480-Cys488) connects loops in the distal end of the RBM.

2019 Novel Coronavirus SARS-CoV-2 is a virus identified as the cause of an outbreak of respiratory illness Covid-19 first detected in Wuhan, China.

To help expedite Covid-19 research, LifeTein synthesized a 69 amino acid spike glycoprotein with one disulfide bond in 6 days. This effort is a partnership with a biotech company for drug development.

Protein Purification Using Magnetic Beads: Top Tips for Success

Magnetic bead-based protein purification offers a powerful solution for various applications like high-throughput microscale purification, pull-down/CoIP experiments, and protein-protein or protein-DNA interaction studies. Here’s why magnetic beads are the top choice: they can be coated with specific affinity ligands for antigens, antibodies, proteins, or nucleic acids. Moreover, magnetic beads are non-porous and have a defined diameter, eliminating hidden surfaces where molecules can stick, leading to reduced background, simplified purification, and streamlined washing steps. Compared to traditional bead separation methods involving agarose, sepharose, or silica beads, magnetic bead separation stands out as the quickest, cleanest, and most efficient technique.

If you’re new to working with magnetic beads, here are some essential tips to ensure success:

1. Thorough Resuspension: Ensure uniformity across aliquots by thoroughly resuspending your magnetic beads. These nano-superparamagnetic beads are covalently coated with highly functional groups, providing increased binding capacity and better dispersion. Since magnetic beads are composed of iron oxide and can settle over time, it’s crucial to vortex and resuspend them thoroughly before use to redisperse the beads.
2. Enhanced Washing: Minimize non-specific binding by increasing the number of washing steps. Whether you’re using ethanol or the recommended wash buffer, make sure to use an adequate volume of wash solution to cover the bead pellet.
3. Understanding Functional Groups: Different beads are covalently coated with various functional groups like maleimide, primary amine, NHS, carboxylic acid, purified streptavidin, protein A, reduced glutathione, nickel-charged nitrilotriacetic acid, or groups for DNA/RNA purification. These coatings, along with buffer conditions, affect bead properties. Understanding these specifics is essential for proper bead handling.
4. Efficient Bead Capture: Magnetic beads typically form a pellet attracted to the magnet within a minute. Extend the attraction time to ensure efficient bead capture.
5. Gentle Supernatant Removal: When removing the wash solution or supernatant, angle the pipette tip to avoid disturbing the magnetic bead pellet. Ensure that the tip doesn’t come into contact with the pellet.

By following these tips, you can make the most of magnetic bead-based protein purification, improving the efficiency and reliability of your experiments.

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)

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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

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