Gersizangitide

Gersizangitide is a peptide combining polar, aromatic, and hydrophobic residues that facilitate diverse secondary structures. The motif is used to study peptide-protein interfaces, hydrogen-bond patterns, and conformational equilibria. Researchers apply it in mechanistic folding studies and structural mapping. Its balanced residue composition supports detailed biophysical analysis.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Gersizangitide(CAS 2417491-82-6)

CAT No: R2319

CAS No:2417491-82-6

Synonyms/Alias:Gersizangitide;2417491-82-6;Gersizangitide [INN];UNII-XBL53GSJ6Y;XBL53GSJ6Y;Leu-Arg-Arg-Phe-Ser-Thr-Ala-Pro-Phe-Ala-Phe-Ile-Asp-Ile-Asn-Asp-Val-Ile-Asn-Phe-NH2;AXT107;GLXC-26939;AKOS040757754;DA-73705;L-Phenylalaninamide, L-leucyl-L-arginyl-L-arginyl-L-phenylalanyl-L-seryl-L-threonyl-L-alanyl-L-prolyl-L-phenylalanyl-L-alanyl-L-phenylalanyl-L-isoleucyl-L-alpha-aspartyl-L-isoleucyl-L-asparaginyl-L-alpha-aspartyl-L-valyl-L-isoleucyl-L-asparaginyl-;

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M.F/Formula
C111H167N29O28
M.W/Mr.
2355.7
Sequence
One Letter Code:LRRFSTAPFAFIDINDVINF
Three Letter Code:H-Leu-Arg-Arg-Phe-Ser-Thr-Ala-Pro-Phe-Ala-Phe-Ile-Asp-Ile-Asn-Asp-Val-Ile-Asn-Phe-NH2

Gersizangitide is a synthetic peptide compound recognized for its potent activity as an integrin antagonist, specifically targeting the αvβ3 and αvβ5 integrins. Structurally, it is engineered to mimic the Arg-Gly-Asp (RGD) motif, a sequence critical for cell adhesion processes mediated by integrins. Its unique biochemical properties have made it an essential research tool in the study of cell-matrix interactions, angiogenesis, and tumor biology. Due to its high selectivity and stability, Gersizangitide is widely utilized in experimental systems seeking to dissect the molecular mechanisms underlying integrin-mediated signaling pathways.

Cell Adhesion Research: Gersizangitide is extensively used in investigations focused on cell adhesion and migration, as it effectively inhibits the binding of cells to extracellular matrix proteins such as vitronectin and fibronectin. By disrupting these interactions, the peptide allows researchers to delineate the role of specific integrins in cellular attachment, spreading, and motility. This application is particularly valuable in studies aiming to elucidate the fundamental processes of tissue development, repair, and pathological remodeling.

Angiogenesis Studies: The compound serves as a critical tool in angiogenesis research, where modulation of integrin activity is essential for understanding new blood vessel formation. By blocking αvβ3 and αvβ5 integrin function, Gersizangitide enables precise interrogation of endothelial cell behavior, proliferation, and migration during neovascularization. This facilitates the identification of molecular regulators and pathways that govern angiogenic responses in physiological and pathological contexts.

Tumor Microenvironment Modeling: In the context of cancer research, Gersizangitide is utilized to model and probe the interactions between tumor cells and their microenvironment. Its ability to antagonize integrin-mediated signaling provides insights into how cancer cells communicate with stromal components, invade surrounding tissues, and establish metastatic niches. The peptide is thus instrumental in preclinical models investigating the dynamics of tumor progression, invasion, and metastasis.

Peptide-Drug Conjugate Development: The specificity of Gersizangitide for integrin receptors makes it a valuable scaffold for the design of peptide-drug conjugates and targeted delivery systems. Researchers employ this peptide as a targeting moiety to direct therapeutic agents or imaging probes to cells expressing high levels of αvβ3 or αvβ5 integrins. Such strategies are pivotal in the development of precision delivery platforms for experimental therapeutics and diagnostics in oncology and vascular biology.

Peptide Structure-Activity Relationship (SAR) Analysis: Gersizangitide is frequently used in structure-activity relationship studies to explore the impact of sequence modifications on integrin binding affinity and selectivity. By systematically altering its amino acid composition or backbone structure, researchers can gain critical insights into the determinants of peptide-receptor interactions. These findings inform the rational design of next-generation integrin antagonists with improved pharmacological profiles for use in basic research and biotechnological applications.

InChI
InChI=1S/C111H167N29O28/c1-14-58(8)86(105(164)132-76(52-82(114)144)98(157)129-77(53-83(145)146)100(159)135-85(57(6)7)104(163)138-88(60(10)16-3)107(166)131-75(51-81(113)143)97(156)126-71(90(115)149)47-64-32-21-17-22-33-64)137-101(160)78(54-84(147)148)133-106(165)87(59(9)15-2)136-99(158)74(50-67-38-27-20-28-39-67)127-91(150)61(11)122-95(154)72(48-65-34-23-18-24-35-65)130-103(162)80-42-31-45-140(80)109(168)62(12)123-108(167)89(63(13)142)139-102(161)79(55-141)134-96(155)73(49-66-36-25-19-26-37-66)128-94(153)70(41-30-44-121-111(118)119)125-93(152)69(40-29-43-120-110(116)117)124-92(151)68(112)46-56(4)5/h17-28,32-39,56-63,68-80,85-89,141-142H,14-16,29-31,40-55,112H2,1-13H3,(H2,113,143)(H2,114,144)(H2,115,149)(H,122,154)(H,123,167)(H,124,151)(H,125,152)(H,126,156)(H,127,150)(H,128,153)(H,129,157)(H,130,162)(H,131,166)(H,132,164)(H,133,165)(H,134,155)(H,135,159)(H,136,158)(H,137,160)(H,138,163)(H,139,161)(H,145,146)(H,147,148)(H4,116,117,120)(H4,118,119,121)/t58-,59-,60-,61-,62-,63+,68-,69-,70-,71-,72-,73-,74-,75-,76-,77-,78-,79-,80-,85-,86-,87-,88-,89-/m0/s1
InChI Key
YVOJSNXOGANXSQ-BZHNYRKKSA-N

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