H
Hiroyasu Ohtaka
Researcher at Johns Hopkins University
Publications - 7
Citations - 955
Hiroyasu Ohtaka is an academic researcher from Johns Hopkins University. The author has contributed to research in topics: Protease & HIV-1 protease. The author has an hindex of 7, co-authored 7 publications receiving 925 citations.
Papers
More filters
Journal ArticleDOI
Isothermal Titration Calorimetry
TL;DR: In this unit several protocols are presented, ranging from the basic ones aimed at characterizing binding of moderate affinity to advanced protocols that are aimed at determining very high or very low affinity binding processes.
Journal ArticleDOI
Compensating enthalpic and entropic changes hinder binding affinity optimization.
Virginie Lafont,Anthony A. Armstrong,Hiroyasu Ohtaka,Yoshiaki Kiso,L. Mario Amzel,Ernesto Freire,Ernesto Freire +6 more
TL;DR: Crystallographic and thermodynamic analysis of the inhibitor/protease complexes indicates that the entropy losses are due to a combination of conformational and solvation effects, providing a set of practical guidelines aimed at overcoming enthalpy/entropy compensation and improve binding potency.
Journal ArticleDOI
Multidrug resistance to HIV-1 protease inhibition requires cooperative coupling between distal mutations.
TL;DR: This paper characterized a multiple-drug-resistant mutant of the HIV-1 protease that affects indinavir, nelfinavIR, saquinavir, ritonavIR, amprenavir and lopinavir and provides a set of thermodynamic guidelines for the design of inhibitors with a lower susceptibility to this type of mutations.
Journal ArticleDOI
Adaptive inhibitors of the HIV-1 protease
Hiroyasu Ohtaka,Ernesto Freire +1 more
TL;DR: A plausible strategy for designing high affinity adaptive inhibitors is to engineer their most critical interactions with conserved regions of the target while allowing for adaptability through the introduction of flexible asymmetric functionalities in places facing variable regions ofThe target.
Journal ArticleDOI
Overcoming drug resistance in HIV-1 chemotherapy: the binding thermodynamics of Amprenavir and TMC-126 to wild-type and drug-resistant mutants of the HIV-1 protease.
TL;DR: Analysis of the data for TMC‐126 and KNI‐764, another second‐generation inhibitor, indicates that their low susceptibility to mutations is caused by their ability to compensate for the loss of interactions with the mutated target by a more favorable entropy of binding.