NDLI: Prospects and limitations of the rational engineering of fibrillar collagens.

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Prospects and limitations of the rational engineering of fibrillar collagens.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dhume, Shirish T. Majsterek, Ireneusz Adachi, Eijiro McAdams, Erin Fertala, Andrzej
Description	Country affiliation: United States Author Affiliation: Majsterek I ( Department of Dermatology and Cutaneous Biology, Jefferson Medical College, Jefferson Institute of Molecular Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.)
Abstract	Recombinant collagens are attractive proteins for a number of biomedical applications. To date, significant progress was made in the large-scale production of nonmodified recombinant collagens; however, engineering of novel collagen-like proteins according to customized specifications has not been addressed. Herein we investigated the possibility of rational engineering of collagen-like proteins with specifically assigned characteristics. We have genetically engineered two DNA constructs encoding multi-D4 collagens defined as collagen-like proteins, consisting primarily of a tandem of the collagen II D4 periods that correspond to the biologically active region. We have also attempted to decrease enzymatic degradation of novel collagen by mutating a matrix metalloproteinase 1 cleavage site present in the D4 period. We demonstrated that the recombinant collagen alpha-chains consisting predominantly of the D4 period but lacking most of the other D periods found in native collagen fold into a typical collagen triple helix, and the novel procollagens are correctly processed by procollagen N-proteinase and procollagen C-proteinase. The nonmutated multi-D4 collagen had a normal melting point of 41 degrees C and a similar carbohydrate content as that of control. In contrast, the mutant multi-D4 collagen had a markedly lower thermostability of 36 degrees C and a significantly higher carbohydrate content. Both collagens were cleaved at multiple sites by matrix metalloproteinase 1, but the rate of hydrolysis of the mutant multi-D4 collagen was lower. These results provide a basis for the rational engineering of collagenous proteins and identifying any undesirable consequences of altering the collagenous amino acid sequences.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	9
Volume Number	12
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2003-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Fibrillar Collagens Chemistry Protein Engineering Amino Acids Binding Sites Bone Morphogenetic Protein 1 Bone Morphogenetic Proteins Carbohydrates Cell Line, Tumor Collagen Extracellular Matrix Metabolism Hydrolysis Matrix Metalloproteinases Metalloendopeptidases Microscopy, Electron Procollagen N-endopeptidase Protein Structure, Secondary Protein Structure, Tertiary Recombinant Proteins Temperature Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s. Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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