Short Peptide Nanofiber Biomaterials Ameliorate Local Hemostatic Capacity of Surgical Materials and Intraoperative Hemostatic Applications in Clinics

Abstract

Short designer self‐assembling peptide (dSAP) biomaterials are a new addition to the hemostat group. It may provide a diverse and robust toolbox for surgeons to integrate wound microenvironment with much safer and stronger hemostatic capacity than conventional materials and hemostatic agents. Especially in noncompressible torso hemorrhage (NCTH), diffuse mucosal surface bleeding, and internal medical bleeding (IMB), with respect to the optimal hemostatic formulation, dSAP biomaterials are the ingenious nanofiber alternatives to make bioactive neural scaffold, nasal packing, large mucosal surface coverage in gastrointestinal surgery (esophagus, gastric lesion, duodenum, and lower digestive tract), epicardiac cell‐delivery carrier, transparent matrix barrier, and so on. Herein, in multiple surgical specialties, dSAP‐biomaterial‐based nano‐hemostats achieve safe, effective, and immediate hemostasis, facile wound healing, and potentially reduce the risks in delayed bleeding, rebleeding, post‐operative bleeding, or related complications. The biosafety in vivo, bleeding indications, tissue‐sealing quality, surgical feasibility, and local usability are addressed comprehensively and sequentially and pursued to develop useful surgical techniques with better hemostatic performance. Here, the state of the art and all‐round advancements of nano‐hemostatic approaches in surgery are provided. Relevant critical insights will inspire exciting investigations on peptide nanotechnology, next‐generation biomaterials, and better promising prospects in clinics.

Humidity-responsive self-assembly of short peptides with super-flexibility

“…In particular, short peptides, characterized by only a few amino acids, exhibit intrinsic conformational flexibility, rendering them highly attractive as building blocks for self-assembly processes. 7 The interplay between the molecular dynamics of these peptides and external stimuli, such as solvent engineering, engenders unique structural transformations. For example, monodispersed diphenylalanine in aqueous solution can assemble into an ordered structure with mechanical rigidity, 8,9 driven primarily by the hydrophobic effect via aromatic organization.…”