Light-Activated Peptide-Based Materials for Sutureless Wound Closure

Abstract

Using chemically modified extracellular matrix proteins, such as collagen, in combination with light for tissue bonding reduces inflammation and minimizes scarring. However, full length animal or recombinant human collagen proteins are difficult to isolate/produce. Thus, short biomimetic collagen peptides with properties equivalent to collagen at both structural and functional levels may be ideal building blocks for the development of remotely triggered adhesives and fillers. In this work, the conjugation of self-assembling collagen-like peptides to acrylate functionalized polyethylene glycol units yielded adhesive filler materials activated by visible light through the incorporation of a photosensitizer. When tested in a murine skin wound model, the photoactivated adhesives showed reduced scar formation and promoted epithelial regeneration.

One‐Pot, Open‐Air Synthesis of Flexible and Degradable Multifunctional Polymer Composites with Adhesion, Water Resistance, Self‐Healing, Facile Drug Loading, and Sustained Release Properties

“…[ 1–3 ] Therefore, effective and timely management of skin wounds remains challenging, especially for extensive or chronic wounds, often requiring additional interventions to promote healing. [ 4–6 ] A common modality currently clinically used to treat skin wounds is to reattach the injured tissue with medical sutures or staples, but it can only protect wounds from external damage and absorb tissue fluid [ 7,8 ] without an obvious therapeutic effect on the inflammation and proliferation stages of wound healing. Hence, designing novel functional wound dressing materials that can resolve the present problems is of the utmost importance in modern medical technology.…”

Self-Organization Dynamics of Collagen-like Peptides Crosslinking Is Driven by Rose-Bengal-Mediated Electrostatic Bridges

“…Biophysical and computational approaches have shown that RB has a binding preference for positive regions of CLPs both to fibers in solution and hydrogel matrices [17,19]. For instances, although CLPI does not present a specific binding site for RB, the formation of an initial binary ground-state complex between RB and one CLP fiber was shown to be driven by electrostatic interactions [20,21]. The main electrostatic interactions are established between the phenolate and carboxylate groups of RB with side chains of lysine (Lys) residues present in CLPI [20,21].…”

“…For instances, although CLPI does not present a specific binding site for RB, the formation of an initial binary ground-state complex between RB and one CLP fiber was shown to be driven by electrostatic interactions [20,21]. The main electrostatic interactions are established between the phenolate and carboxylate groups of RB with side chains of lysine (Lys) residues present in CLPI [20,21]. This initial binary ground-state complex represents a crucial step for the effective covalent crosslinking process of CLPI in the presence of RB.…”

“…On the other hand, collagen-like peptide II (CLPII) has also been successfully used in PTB therapies in the presence of RB. McTiernan et al showed that RB forms a stable binary ground-state complex with CLPII and that the RB-CLPII ground-state complex presents a higher stability than the RB-CLPI ground-state complex [21]. The higher stability of the RB-CLPII complex can be because-in addition to the electrostatic interactions established between the phenolate and carboxylate groups of RB and the Arginine (Arg) residue in the specific integrin-binding motif ([GFOGER] domain) of CLPII-RB would also establish another type of interaction with RB [21].…”