Genitourinary System

Chandra, Prafulla; Atala, Anthony

doi:10.1016/b978-0-12-801238-3.65846-4

Cited by 1 publication

(2 citation statements)

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“…As a complex biopolymer network, the ECM accommodates several biochemical interactions and impacts the physical environment for various physiological processes including pathological and healing states. Collagen matrices are frequently used in biomaterials that are developed for tissue engineering applications [ 2 , 3 ]. Among the 28 subtypes of collagen identified to date, 90% of collagen in the human body is COL1 [ 3 ].…”

Section: Introductionmentioning

confidence: 99%

“…Collagen matrices are frequently used in biomaterials that are developed for tissue engineering applications [ 2 , 3 ]. Among the 28 subtypes of collagen identified to date, 90% of collagen in the human body is COL1 [ 3 ]. Among the many interacting partners with collagen are extracellular matrix components [ 4 , 5 ], decorin [ 6 , 7 ], and other leucine-rich repeat (LRR) proteins [ 8 ].…”

Section: Introductionmentioning

confidence: 99%

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Designing Collagen-Binding Peptide with Enhanced Properties Using Hydropathic Free Energy Predictions

et al. 2023

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Collagen is fundamental to a vast diversity of health functions and potential therapeutics. Short peptides targeting collagen are attractive for designing modular systems for site-specific delivery of bioactive agents. Characterization of peptide–protein binding involves a larger number of potential interactions that require screening methods to target physiological conditions. We build a hydropathy-based free energy estimation tool which allows quick evaluation of peptides binding to collagen. Previous studies showed that pH plays a significant role in collagen structure and stability. Our design tool enables probing peptides for their collagen-binding property across multiple pH conditions. We explored binding features of currently known collagen-binding peptides, collagen type I alpha chain 2 sense peptide (TKKTLRT) and decorin LRR-10 (LRELHLNNN). Based on these analyzes, we engineered a collagen-binding peptide with enhanced properties across a large pH range in contrast to LRR-10 pH dependence. To validate our predictions, we used a quantum-dots-based binding assay to compare the coverage of the peptides on type I collagen. The predicted peptide resulted in improved collagen binding. Hydropathy of the peptide–protein pair is a promising approach to finding compatible pairings with minimal use of computational resources, and our method allows for quick evaluation of peptides for binding to other proteins. Overall, the free-energy-based tool provides an alternative computational screening approach that impacts protein interaction search methods.

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Section: Introductionmentioning

confidence: 99%