Identification of small peptides and glycinamide that inhibit melanin synthesis using a positional scanning synthetic peptide combinatorial library

2019 ◽  
Vol 181 (1) ◽  
pp. 128-137 ◽  
Author(s):  
J. H. Kim ◽  
J. K. Seok ◽  
Y. M. Kim ◽  
Y. C. Boo

2016 ◽  
Vol 100 ◽  
pp. S81
Author(s):  
Jin Kyung Seok ◽  
Seok Won Lee ◽  
Young Mi Kim ◽  
Yong Chool Boo


2017 ◽  
Vol 26 (8) ◽  
pp. 742-744 ◽  
Author(s):  
Jin K. Seok ◽  
Seok W. Lee ◽  
Jaehyuk Choi ◽  
Young M. Kim ◽  
Yong C. Boo


Peptides 1992 ◽  
1993 ◽  
pp. 65-66
Author(s):  
Clemencia Pinilla ◽  
Jon R. Appel ◽  
Richard A. Houghten


2012 ◽  
Vol 393 (5) ◽  
pp. 331-341 ◽  
Author(s):  
Simon J. de Veer ◽  
Joakim E. Swedberg ◽  
Edward A. Parker ◽  
Jonathan M. Harris

Abstract An array of substrates link the tryptic serine protease, kallikrein-related peptidase 14 (KLK14), to physiological functions including desquamation and activation of signaling molecules associated with inflammation and cancer. Recognition of protease cleavage sequences is driven by complementarity between exposed substrate motifs and the physicochemical signature of an enzyme’s active site cleft. However, conventional substrate screening methods have generated conflicting subsite profiles for KLK14. This study utilizes a recently developed screening technique, the sparse matrix library, to identify five novel high-efficiency sequences for KLK14. The optimal sequence, YASR, was cleaved with higher efficiency (kcat/Km=3.81±0.4×106 m-1 s-1) than favored substrates from positional scanning and phage display by 2- and 10-fold, respectively. Binding site cooperativity was prominent among preferred sequences, which enabled optimal interaction at all subsites as indicated by predictive modeling of KLK14/substrate complexes. These simulations constitute the first molecular dynamics analysis of KLK14 and offer a structural rationale for the divergent subsite preferences evident between KLK14 and closely related KLKs, KLK4 and KLK5. Collectively, these findings highlight the importance of binding site cooperativity in protease substrate recognition, which has implications for discovery of optimal substrates and engineering highly effective protease inhibitors.



2003 ◽  
Vol 5 (5) ◽  
pp. 597-605 ◽  
Author(s):  
Marc Humet ◽  
Teresa Carbonell ◽  
Isabel Masip ◽  
Francisco Sánchez-Baeza ◽  
Puig Mora ◽  
...  


2016 ◽  
Vol 108 ◽  
pp. 354-363 ◽  
Author(s):  
Nina Bionda ◽  
Renee M. Fleeman ◽  
César de la Fuente-Núñez ◽  
Maria C. Rodriguez ◽  
Fany Reffuveille ◽  
...  




ImmunoMethods ◽  
1992 ◽  
Vol 1 (1) ◽  
pp. 17-23 ◽  
Author(s):  
Jon R. Appel ◽  
Clemencia Pinilla ◽  
Richard A. Houghten


Peptides 1992 ◽  
1993 ◽  
pp. 903-904
Author(s):  
Clemencia Pinilla ◽  
Jon R. Appel ◽  
Sandry Chendra ◽  
Richard A. Houghten


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