Isolation of cathepsin B inhibitory peptides, Cabin-A1 and -A2, from a tryptic and chymotryptic hydrolysate of human serum albumin.
Two novel peptides that inhibit cathepsin B were isolated from a tryptic and chymotryptic hydrolysate of human serum albumin, and designated as Cabin-A1 and -A2. Cabin-A1 and -A2 were purified by reversed-phase HPLC and identified as Ser-Leu-His-Thr-Leu-Phe and Phe-Gln-Asn-Ala-Leu, respectively. These peptides correspond to f(65-70) and f(403-407) of human serum albumin. Human albutensin A (Ala-Phe-Lys-Ala-Trp-Ala-Val-Ala-Arg), which corresponds to f(210-218), was also isolated as a potent cathepsin B inhibitor. Synthetic Cabin-A1, -A2, and human albutensin A showed dose-dependent inhibition of cathepsin B, with K(i) values of 2.4, 290, and 3.8 microM, respectively.
Nakagomi
Kazuya
K
Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama, Japan. nakagomi@pharm.teikyo-u.ac.jp
Takatsu
Kouki
K
Takagi
Shinobu
S
Ebisu
Hidetoshi
H
Sadakane
Yutaka
Y
Fujii
Noriko
N
Akizawa
Toshifumi
T
Tanimura
Takenori
T
Hatanaka
Yasumaru
Y
D002401:Cathepsin B / Q000037:antagonists & inhibitors* / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D006801:Humans; D007700:Kinetics; D009842:Oligopeptides / Q000302:isolation & purification* / Q000494:pharmacology; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification*; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism; D013997:Time Factors; D014357:Trypsin / Q000494:pharmacology
D009842:Oligopeptides; D010455:Peptides; D012709:Serum Albumin; C418002:albutensin A; C468309:cabin-1; C468308:cabin-2; D002918:Chymotrypsin; D014357:Trypsin; D002401:Cathepsin B