Protein conformational changes induced by adsorption onto material surfaces: an important issue for biomedical applications of material science

Bulletin of the Polish Academy of Sciences. Technical Sciences

L. BoulangeBecton-Dickinson Pharmaceutical Systems, 11 Avenue Aristide Bergès, 38800 Le Pont de Claix, FranceOther articles by this author:De Gruyter OnlineGoogle Scholar¹  Y. BrechetLaboratoire de Science et Ingénierie des Matériaux et Procédés, Grenoble Institute of Technology, 1130 rue de la Piscine, BP 75, 38402 Saint Martin d'Hères Cedex, FranceOther articles by this author:De Gruyter OnlineGoogle Scholar²  F. BruckertLaboratoire des Matériaux et du Génie Physique, Grenoble Institute of Technology Minatec, 3, Parvis Louis Néel, BP 257, 38016 Grenoble Cedex 1, FranceOther articles by this author:De Gruyter OnlineGoogle Scholar³  M. WeidenhauptLaboratoire des Matériaux et du Génie Physique, Grenoble Institute of Technology Minatec, 3, Parvis Louis Néel, BP 257, 38016 Grenoble Cedex 1, FranceOther articles by this author:De Gruyter OnlineGoogle Scholar³  T. BalletLaboratoire des Matériaux et du Génie Physique, Grenoble Institute of Technology Minatec, 3, Parvis Louis Néel, BP 257, 38016 Grenoble Cedex 1, FranceBecton-Dickinson Pharmaceutical Systems, 11 Avenue Aristide Bergès, 38800 Le Pont de Claix, FranceOther articles by this author:De Gruyter OnlineGoogle Scholar³ 

[1] Becton-Dickinson Pharmaceutical Systems, 11 Avenue Aristide Bergès, 38800 Le Pont de Claix, France;Laboratoire de Science et Ingénierie des Matériaux et Procédés, Grenoble Institute of Technology, 1130 rue de la Piscine, BP 75, 38402 Saint Martin d'Hères Cedex, France;Laboratoire des Matériaux et du Génie Physique, Grenoble Institute of Technology Minatec, 3, Parvis Louis Néel, BP 257, 38016 Grenoble Cedex 1, France

关键词: Keywords: protein;    conformation;    unfolding;    aggregation;    material surface;    nanostructure;   

DOI  :  10.2478/v10175-010-0028-0

学科分类：工程和技术（综合）

来源: Polska Akademia Nauk * Centrum Upowszechniania Nauki / Polish Academy of Sciences, Center for the Advancement of Science

【 摘 要 】

Protein adsorption on solid surfaces is a widespread phenomenon of large biological and biotechnological significance. Conformational changes are likely to accompany protein adsorption, but are difficult to evidence directly. Nevertheless they have important consequences, since the partial unfolding of protein domains can expose hitherto hidden amino acids. This remodeling of the protein surface can trigger the activation of molecular complexes such as the blood coagulation cascade or the innate immune complement system. In the case of extracellular matrix, it can also change the way cells interact with the material surfaces and result in modified cell behavior. In this review, we present direct and indirect evidences that support the view that some proteins change their conformation upon adsorption. We also show that both physical and chemical methods are needed to study the extent and kinetics of protein conformational changes. In particular, AFM techniques and cryo-electron microscopy provide useful and complementary information. We then review the chemical and topological features of both proteins and material surfaces in relation with protein adsorption. Mutating key amino acids in proteins changes their stability and this is related to material-induced conformational changes, as shown for instance with insulin. In addition, combinatorial methods should provide valuable information about peptide or antibody adsorption on well-defined material surfaces. These techniques could be combined with molecular modeling methods to decipher the rules governing conformational changes associated with protein adsorption.

【 授权许可】

Unknown