Design and Production of a Chimeric Resilin-, Elastin-, and Collagen-Like Engineered Polypeptide

被引:79
作者
Bracalello, Angelo [1 ]
Santopietro, Valentina [1 ]
Vassalli, Massimo [2 ]
Marletta, Giovanni [3 ]
Del Gaudio, Rosanna [4 ]
Bochicchio, Brigida [1 ]
Pepe, Antonietta [1 ]
机构
[1] Univ Basilicata, Dept Chem Antonio M Tamburrro, I-85100 Potenza, Italy
[2] Natl Res Council Italy, Inst Biophys, I-16149 Genoa, Italy
[3] Univ Catania, Dept Chem Sci, I-95125 Catania, Italy
[4] Univ Naples Federico II, Dept Biol Sci, I-80134 Naples, Italy
关键词
STRUCTURAL-CHARACTERIZATION; ATOMIC-FORCE; MECHANICAL-PROPERTIES; EXTRACELLULAR-MATRIX; PHYSICAL-PROPERTIES; CHEMICAL SYNTHESIS; PROTEIN POLYMER; BIOMATERIALS; MODEL; BIOPOLYMERS;
D O I
10.1021/bm2005388
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein-inspired biomaterials have gained great interest as an alternative to synthetic polymers, in particular, for their potential use as biomedical devices. The potential inspiring models are mainly proteins able to confer mechanical properties to tissues and organs, such as elasticity (elastin, resilin, spider silk) and strength (collagen, silk). The proper combination of repetitive sequences, each of them derived from different proteins, represents a useful tool for obtaining biomaterials with tailored mechanical properties and biological functions. In this report we describe the design, the production, and the preliminary characterization of a chimeric polypeptide, based on sequences derived from the highly resilient proteins resilin and elastin and from collagen-like sequences. The results show that the obtained chimeric recombinant material exhibits promising self-assembling properties. Young's modulus of the fibers was determined by AFM image analysis and lies in the range of 0.1-3 MPa in agreement with the expectations for elastin-like and resilin-like materials.
引用
收藏
页码:2957 / 2965
页数:9
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