Synthesis and characterization of some collagen sequence analogs.
Some analogs of natural collagen sequences (773-779) were synthesized. The peptides were hydrolyzed at the Gly-Ile bond not only by crude collagenase isolated from normal rat liver, but also by the bacterial Clostridium histolyticum collagenase. The reason for this unusual cleavage site in the latter case may lie in the unordered secondary structure of the substrates measured by CD spectroscopy.
Botyánszki
J
J
Res. Group of Peptide Chemistry, Hung. Acad. Sci., Budapest.
Bódi
J
J
Kajtár
J
J
Ragnarsson
U
U
Pogány
G
G
Jeney
A
A
Süli-Vargha
H
H
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism; D002942:Circular Dichroism; D003013:Clostridium / Q000201:enzymology; D003094:Collagen / Q000031:analogs & derivatives*; D017364:Collagenases / Q000378:metabolism; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis* / Q000378:metabolism; D011487:Protein Conformation
D001426:Bacterial Proteins; D010446:Peptide Fragments; D003094:Collagen; D017364:Collagenases