Inhibition of Collagenase from Achromobacter iophagus by Synthetic Peptides

Synthetic peptides as inactivators of multimeric enzymes: inhibition of Plasmodium falciparum triosephosphate isomerase by interface peptides.

Synthetic peptides corresponding to two distinct segments of the subunit interface of the homodimeric enzyme triosephosphate isomerase (residues 9-18, ANWKCNGTLE, peptide I; residues 68-79, KFGNGSYTGEVS, peptide II) from Plasmodium falciparum (PfTIM) have been investigated for their ability to act as inhibitors by interfering with the quaternary structure of the enzyme. An analog of peptide II ...

Inhibition of Molt-4-endothelial adherence by synthetic peptides from the sequence of ICAM-1.

Previous studies have shown that inflammatory pathologies are mediated by lymphocyte adhesion to endothelium and subsequent transmigration through the endothelial monolayer. Lymphocyte-endothelial adherence is, in part, caused by the leukocyte integrin LFA-1 binding to ICAM-1, its ligand on endothelial cells. Synthetic peptides based on specific amino acid sequences of human ICAM-1 inhibit the ...

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

Cleavage specificity of type IV collagenase (gelatinase) from human skin. Use of synthetic peptides as model substrates.

Type IV collagenase (gelatinase) has a marked substrate specificity for denatured collagen (gelatin). Cleavage site specificity of type IV collagenase from human skin was determined using small collagenous peptides with varied sequences around Gly-Leu or Gly-Ile. Type IV collagenase showed essentially the same order of preference for the peptide substrates as did interstitial collagenase. Both ...