Comparative 1H NMR studies on the structural looseness of the aged (A) and non-aged (N) bovine mercaptalbumin in the alkaline region

Era, Seiichi; Sogami, Masaru; Kuwata, Kazuo

doi:10.1016/j.ijbiomac.2008.09.021

Cited by 3 publications

(1 citation statement)

References 41 publications

(188 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The N(normal)-A(aged) isomerization leads to the structural relaxation of the protein structure. It mainly affects the N-terminal region and thereby may influence the ligand binding affinity [ 4 , 5 ]. The A(aged) form of bovine serum albumin (ABSA) was first described by Nikkel and Foster [ 6 ].…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic Studies on the Molecular Ageing of Serum Albumin

et al. 2016

View full text Add to dashboard Cite

Pathological states in the organism, e.g., renal or hepatic diseases, cataract, dysfunction of coronary artery, diabetes mellitus, and also intensive workout, induce the structural modification of proteins called molecular ageing or N-A isomerization. The aim of this study was to analyze the structural changes of serum albumin caused by alkaline ageing using absorption, spectrofluorescence, and circular dichroism spectroscopy. The N-A isomerization generates significant changes in bovine (BSA) and human (HSA) serum albumin subdomains—the greatest changes were observed close to the tryptophanyl (Trp) and tyrosyl (Tyr) residue regions while a smaller change was observed in phenyloalanine (Phe) environment. Moreover, the changes in the polarity of the Trp neighborhood as well as the impact of the ageing process on α-helix, β-sheet content, and albumin molecule rotation degree have been analyzed. Based on the spectrofluorescence study, the alterations in metoprolol binding affinity to the specific sites that increase the toxicity of the drug were investigated.

show abstract

Section: Introductionmentioning

confidence: 99%