Elucidating pH-Dependent Collagen Triple Helix Formation through Interstrand Hydroxyproline-Glutamic Acid Interactions

被引:6
|
作者
Chen, Liwei [1 ]
Cai, Shuting [1 ]
Lim, Jaehong [1 ]
Lee, Su Seong [1 ]
Lee, Song-Gil [1 ]
机构
[1] Inst Bioengn & Nanotechnol, Singapore 138669, Singapore
关键词
collagen; hydrogen bonding; hydroxyproline; peptides; pH switches; I COLLAGEN; THERMAL-STABILITY; PEPTIDE; SEQUENCE; BIOSYNTHESIS; CONFORMATION; PREFERENCES; RESIDUES; FIBRILS; MODEL;
D O I
10.1002/cbic.201402570
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
Here, we describe systematic explorations into the molecular basis underlying hydroxyproline-mediated interstrand interactions on the triple-helical stability of collagen-mimetic peptides containing glutamic acid residues. Our studies reveal that the triple-helical stability of these peptides relies on the existence of interstrand interactions between hydroxyprolines and glutamic acid residues that are pH dependent. These unique interactions have been used to engineer collagen peptides that form triple helices on demand through pH control.
引用
收藏
页码:407 / 410
页数:4
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