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pubs.acs.org/biochemistry
TheaA66-80PeptideInteractswithSolublea-CrystallinandInduces
Its Aggregation and Precipitation: A Contribution to Age-Related
Cataract Formation
† ‡ § ,†,‡
Rama Kannan, Puttur Santhoshkumar, Brian P. Mooney, and K. Krishna Sharma*
†
Department of Biochemistry, University of Missouri, Columbia, Missouri 65211, United States
‡
Department of Ophthalmology, University of Missouri School of Medicine, Columbia, Missouri 65212, United States
§
Charles W. Gehrke Proteomics Center, University of Missouri, Columbia, Missouri 65211, United States
S
*Supporting Information
ABSTRACT: Formation of protein aggregates in the aging
eye lens has been shown to correlate with progressive
accumulation of speci?c low-molecular weight (LMW)
peptides derived from crystallins. Prominent among the
LMW fragments is aA66-80, a peptide derived from aA-
crystallin and present at higher concentrations in the water-
insoluble nuclear fractions of the aging lens. The aA66-80
peptide has amyloid-like properties and preferentially insolubilizes a-crystallin from soluble lens fractions. However, the speci?c
interactionsandmechanismsbywhichthepeptideinducesa-crystallinaggregationhavenotbeendelineated.Togaininsightinto
the mechanisms of peptide-induced aggregation, we investigated the interactions of the peptide with a-crystallin by various
biochemical approaches. The peptide weakens a-crystallin chaperone ability and drastically promotes a-crystallin aggregation via
the formation of insoluble peptide-protein complexes through transient intermediates. 4,4'-Dianilino-1,1'-binaphthyl-5,5'-
disulfonic acid studies suggest that the peptide induces changes in the hydrophobicity of a-crystallin that could trigger the
formation and growth of aggregates. The peptide-a-crystallin aggregates were found to be resistant to dissociation by high ionic
strengths, whereas guanidinium hydrochloride and urea were e?ective dissociating agents. We conclude that the aA66-80
peptide forms...

David · Accepted Answer

Covalent Inhibition of Serine β‑Lactamases by Novel Hydroxamic Acid Derivatives 
INTRODUCTION: β -lactam antibiotics are widely used in medicine for antibiotic activity 
against variety of Gram positive and negative bacteria. The basic structure of these class 
antibiotics contains a β-lactam ring and the activity of the molecule is due to the presence of 
this ring. But certain enzymes present in bacteria called β – lactamases causes the breaking of 
this ring and the molecule loses its activity. This leads to increases bacterial resistance to the 
antibiotic agent. So compounds that inhibit β – lactamases should be developed to contain the 
crucial issue of antibiotic resistance. Non-covalent β – lactamase inhibitors are not much 
effective against this drug resistance, as this enzyme has a broad range of action against the 
lactamide ring. Therefore, covalent β – lactamase inhibitors are widely used to serve the 
purpose along with the antibiotic drug. Most of the β – lactamase inhibitors work as acylating 
agents, phosphylating agents, sulphonating agents and boronic acids. The authors have 
reported the use of certain compound before which act as an acylating agent, which shoes 
siginificant β – lactamase inhibition. That study showed that the candidate molecule inhibited 
class C Enterobacter cloacae P99 β – lactamase and the inhibitory mechanism involves 
nucleophilic attack on the reactive carbonyl group by the active site serine hydroxyl, which is 
followed by the loss of aryloxide group to get acyl-enzyme.

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