Synthetic Peptides Mimic the Assembly of Transmembrane Glycoproteins

Synthetic disulfide-bridged cyclic peptides mimic the anti-angiogenic actions of chondromodulin-I

Chondromodulin-I (ChM-I) is a 25-kDa glycoprotein in cartilage matrix that inhibits angiogenesis. It contains two distinctive structural domains: the N-terminal third of the molecule is a hydrophilic domain that contains O-linked and N-linked oligosaccharide chains, and the C-terminal two-thirds is a hydrophobic domain that contains all of the cysteine residues. In the present study, we have at...

In vitro inhibition of feline leukaemia virus infection by synthetic peptides derived from the transmembrane domain.

BACKGROUND The feline leukaemia virus (FeLV) is a gammaretrovirus commonly affecting cats. Infection with this virus often leads to fatal outcomes and, so far, no cure is available for this disease. Synthetic peptides with structures mimicking the transmembrane protein of the viral surface proteins hold the potential to effectively interfere with viral entry by hampering the fusion of viral and...

In vitro Inhibition of Feline Leukaemia Virus Infection by Synthetic Peptides Derived from the Transmembrane Domain

Transmembrane orientation of the glycoproteins in normal human erythrocytes.

Different membrane anchoring positions of tryptophan and lysine in synthetic transmembrane alpha-helical peptides.

Specific interactions of membrane proteins with the membrane interfacial region potentially define protein position with respect to the lipid environment. We investigated the proposed roles of tryptophan and lysine side chains as "anchoring" residues of transmembrane proteins. Model systems were employed, consisting of phosphatidylcholine lipids and hydrophobic alpha-helical peptides, flanked e...