4 Results for "

α-helical content

" in MedChemExpress (MCE) Product Catalog:
Products (4)

4 Results for "α-helical content" in MCE Product Catalog:

1
1 Cited Publications
Cat. No.: HY-P3343A
Target:  

Estrogen Receptor/ERR

Research Areas:  

Endocrinology

hFSH-β-(33-53) TFA is a polypeptide corresponding to residues 33-53 of hFSH-β, and also a follicle-stimulating hormone (FSH) antagonist. hFSH-β-(33-53) stimulates basal estradiol synthesis in cells. hFSH-β-(33-53) TFA prolongs vaginal estrus in mice with normal estrous cycles .
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1
1 Cited Publications
Cat. No.: HY-P3343
CAS No.: 142154-55-0
Target:  

Estrogen Receptor/ERR

Research Areas:  

Endocrinology

hFSH-β-(33-53) is a polypeptide corresponding to residues 33-53 of hFSH-β, and also a follicle-stimulating hormone (FSH) antagonist. hFSH-β-(33-53) stimulates basal estradiol synthesis in cells. hFSH-β-(33-53) prolongs vaginal estrus in mice with normal estrous cycles .
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Cat. No.: HY-W006886
CAS No.: 945212-26-0
Research Areas:  

Others

Fmoc-(R)-2-(7-octenyl) Ala-OH is an unnatural Fmoc-protected amino acid and modification module. Fmoc-(R)-2-(7-octenyl) Ala-OH serves as a key building block for all-hydrocarbon cross-linking modification of antimicrobial peptides, and facilitates the generation of stapled peptide derivatives. When introduced into specific sites of the parent peptide, Fmoc-(R)-2-(7-octenyl) Ala-OH effectively increases the α-helix content of the peptide chain, thereby significantly enhancing its antimicrobial activity and proteolytic stability. Fmoc-(R)-2-(7-octenyl) Ala-OH is widely used in research on bacterial infections and the development of related antimicrobial agents . Stapled peptide is a specially chemically modified polypeptide. It locks the peptide chain into a stable α-helical structure by introducing a "staple"-like chemical bridge (usually an all-carbon backbone) at specific positions of the peptide chain.
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Cat. No.: HY-P11353
CAS No.: 117138-19-9
Research Areas:  

Infection Cancer

HA2 peptide is a potent pH-responsive fusion peptide derived from hemagglutinin (HA), corresponding to the N-terminal fusion peptide domain consisting of 23 amino acid residues of HIV-1 gp41 envelope glycoprotein. HA2 peptide adopts a random coil structure under physiological pH conditions; in acidic endosomes, protonation of carboxyl groups reduces negative charge, inducing a transition to an α-helical conformation that can fuse with and destabilize the endosomal membrane. After binding to membranes, the N-terminal and middle regions of HA2 peptide mainly adopt a β-strand conformation, while the C-terminal region remains unstructured. HA2 peptide induces lipid mixing and promotes aqueous content leakage from large unilamellar vesicles whose lipid composition matches that of HIV-1 viruses and target T cells. HA2 peptide is anionic and can bind to cationic peptides to achieve siRNA condensation. HA2 peptide can be used in studies related to cancer and human immunodeficiency virus (HIV) infection .
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