Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Abhishek A. Jalan"'
Autor:
Katherine Stott, Samir W. Hamaia, Birgit Leitinger, Douglas R. Walker, Jeffrey D. Hartgerink, Douglas Sammon, Paul Brear, Richard W. Farndale, Abhishek A. Jalan, Emma Hunter
Publikováno v:
Nature chemical biology
The most abundant member of the collagen protein family, collagen I (also known as type I collagen; COL1), is composed of one unique (chain B) and two similar (chain A) polypeptides that self-assemble with one amino acid offset into a heterotrimeric
Autor:
Richard W. Farndale, Douglas R. Walker, Jeffrey D. Hartgerink, I-Che Li, Abhishek A. Jalan, Sarah A. H. Hulgan
Publikováno v:
Organic Letters. 21:5480-5484
Stabilizing the three-dimensional structure of supramolecular materials can be accomplished through covalent capture of the assembled system. The lysine-aspartate charge pairs designed to direct the self-assembly of a collagen triple helix were subse
Autor:
Abigael J. Kosgei, I-Che Li, Douglas R. Walker, Mitchell D. Miller, Jeffrey D. Hartgerink, Sarah A. H. Hulgan, Weijun Xu, George N. Phillips, Abhishek A. Jalan
Publikováno v:
Biomacromolecules. 21(9)
Collagen mimetic peptides (CMPs) self-assemble into a triple helix reproducing the most fundamental aspect of the collagen structural hierarchy. They are therefore important for both further understanding this complex family of proteins and use in a
Autor:
Jeffrey D. Hartgerink, Biplab Sarkar, Navindee C. Wickremasinghe, Benjamin K. Wang, Abhishek A. Jalan, Siyu Shi, Vivek A. Kumar, I-Che Li
Publikováno v:
Journal of the American Chemical Society. 137:4823-4830
Self-assembly of multidomain peptides (MDP) can be tailored to carry payloads that modulate the extracellular environment. Controlled release of growth factors, cytokines, and small-molecule drugs allows for unique control of in vitro and in vivo res
Autor:
Nichole L. Taylor, Marci K. Kang, Navindee C. Wickremasinghe, Siyu Shi, Jeffrey D. Hartgerink, Abhishek A. Jalan, Benjamin K. Wang, Vivek A. Kumar
Publikováno v:
ACS Nano. 9:860-868
Major limitations of current tissue regeneration approaches using artificial scaffolds are fibrous encapsulation, lack of host cellular infiltration, unwanted immune responses, surface degradation preceding biointegration, and artificial degradation
Publikováno v:
Journal of the American Chemical Society. 136:7535-7538
In a canonical collagen triple helix, three peptides self-assemble into a supercoiled motif with a one-amino-acid offset between the peptide chains. Design of triple helices that contain more than one residue offset is lucrative, as it leaves the non
Autor:
Vivek A. Kumar, Benjamin K. Wang, Jeffrey D. Hartgerink, Nichole L. Taylor, Lyahn K. Hwang, Abhishek A. Jalan
Publikováno v:
Biomacromolecules
Collagen is a major component of the extracellular matrix and plays a wide variety of important roles in blood clotting, healing, and tissue remodeling. Natural, animal derived, collagen is used in many clinical applications but concerns exist with r
Publikováno v:
Biomacromolecules. 14:179-185
Control over composition and register of the peptide chains in AAB-type collagen mimetic heterotrimers is critical in developing systems that show fidelity to native collagen. However, their design is challenging due to the eight competing states pos
Publikováno v:
Journal of the American Chemical Society. 134:1430-1433
Design of heterotrimeric ABC collagen triple helices is challenging due to the large number of competing species that may be formed. Given the required one amino acid stagger between adjacent peptide strands in this fold, a ternary mixture of peptide
Publikováno v:
Biomacromolecules. 16(1)
The collagen triple helix consists of three supercoiled solvent-exposed polypeptide chains, and by dry weight it is the most abundant fold in mammalian tissues. Many factors affecting the structure and stability of collagen have been determined throu