Structure-activity relationships of peptide T-related pentapeptides.
Fifteen pentapeptide analogs of C-terminal fragment of peptide T, H-Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr-OH, were prepared and tested for human monocyte chemotaxis. Structure-activity studies suggest that the potent chemotactic activity of H-Thr-Thr-Asn-Tyr-Thr-OH is mediated through the polar properties of the C-terminal carboxyl group and Thr side chains at the critical positions 5 and 8, while the hydroxyl group of N-terminal Thr and its free amino function are not essential requirements for CD4 receptor interactions.
Marastoni
M
M
Department of Pharmaceutical Sciences, University of Ferrara, Italy.
Salvadori
S
S
Balboni
G
G
Spisani
S
S
Gavioli
R
R
Traniello
S
S
Tomatis
R
R
D015704:CD4 Antigens / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D002627:Chemistry, Physical; D002633:Chemotaxis / Q000187:drug effects*; D006801:Humans; D066298:In Vitro Techniques; D009000:Monocytes / Q000187:drug effects; D015717:Peptide T / Q000138:chemical synthesis / Q000378:metabolism / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D015704:CD4 Antigens; D015717:Peptide T