Details

Autor(en) / Beteiligte

• Ray, Namrata
• Roy, Sarita
• Singha, Santiswarup
• Chandra, Bappaditya
• Dasgupta, Anjan Kr
• Sarkar, Amitabha

Titel

Design of Heat Shock-Resistant Surfaces to Prevent Protein Aggregation: Enhanced Chaperone Activity of Immobilized α‑Crystallin

Ist Teil von

• Bioconjugate chemistry, 2014-05, Vol.25 (5), p.888-895

Ort / Verlag

United States: American Chemical Society

Erscheinungsjahr

2014

Quelle

MEDLINE

Beschreibungen/Notizen

• α-Crystallin is a multimeric protein belonging to the family of small heat shock proteins, which function as molecular chaperones by resisting heat and oxidative stress induced aggregation of other proteins. We immobilized α-Crystallin on a self-assembled monolayer on glass surface and studied its activity in terms of the prevention of aggregation of aldolase. We discovered that playing with grafted protein density led to interesting variations in the chaperone activity of immobilized α-Crystallin. This result is in accordance with the hypothesis that dynamicity of subunits plays a vital role in the functioning of α-Crystallin and might be able to throw light on the structure–activity relationship. We showed that the chaperone activity of a certain number of immobilized α-Crystallins was superior compared to a solution containing an equivalent number of the protein and 10 times the number of the protein at temperatures >60 °C. The α-Crystallin grafted surfaces retained activity on reuse. This could also lead to the design of potent heat-shock resistant surfaces that can find wide applications in storage and shipping of protein based biopharmaceuticals.