Tailorable and biocompatible collagen-based peptides as distinctive surfactants with micellar self-assembly.

Surface-active peptides (SAPs) typically mimic conventional surfactants by featuring long non-polar (hydrophobic) peptide tails and short polar (hydrophilic) heads consisting of a single amino acid or short peptide. However, reverse-structure SAPs-with a long hydrophilic tail and short hydrophobic head-remain largely unexplored. If developed, such SAPs could form micelles with a larger hydrophilic area and a smaller hydrophobic core, leading to novel self-assembled structures.

Hyperstable and Fibril-Forming Collagen-Mimetic Peptides in Shortest Triple Helices: Empowering the Capping by π-systems.

Developing collagen-mimetic peptides (CMPs) with short triple helices and fibril-forming ability remains challenging. Herein, we stabilized short CMPs (3-6 GPO repeats) by attaching extended aromatic π-system─fluorenyl groups at the N-terminus and tyrosine at the C-terminus. These modifications promoted triple helix folding through π-π interactions, acting as a "glue" to stabilize the structure and facilitate fibrillation.

Dual-Functional Antibiotic Adjuvant Displays Potency against Complicated Gram-Negative Bacterial Infections and Exhibits Immunomodulatory Properties.

The treatment of Gram-negative bacterial infections is challenged by antibiotic resistance and complicated forms of infection like persistence, multispecies biofilms, intracellular infection, as well as infection-associated hyperinflammation and sepsis. To overcome these challenges, a dual-functional antibiotic adjuvant has been developed as a novel strategy to target complicated forms of bacterial infection and exhibit immunomodulatory properties. The lead adjuvant, D-LBDiphe showed multimodal mechanisms of action like weak outer membrane permeabilization, weak membrane depolarization, and inhibition of efflux machinery, guided primarily by hydrogen bonding and electrostatic interactions, along with weak van der Waals forces.

A bio-inspired silkworm 3D cocoon-like hierarchical self-assembled structure from π-conjugated natural aromatic amino acids.

The formation of spontaneous 3D self-assembled hierarchical structures from 1D nanofibers is a significant breakthrough in materials science. Overcoming the major challenges associated with developing these 3D structures, such as uncontrolled self-assembly, complex procedures, and machinery, has been a formidable task. However, the current discovery reveals that simple π-system (fluorenyl)-functionalized natural aromatic amino acids, phenylalanine (Fmoc-F) and tyrosine (Fmoc-Y), can form bio-inspired 3D cocoon-like structures.

Collagen Mimicry with a Short Collagen Model Peptide.

Mimicking triple helix and fibrillar network of collagen through collagen model peptide(CMP) with short GPO tripeptide repeats is a great challenge. Herein, a minimalistic CMP comprising only five GPO repeats [(GPO) ] is presented. This novel approach involves the fusion of ultrashort peptide with the synergetic power of π-system and β-sheet formation to short CMP (GPO) .

Impact of SiO nanoparticles on the structure and property of type I collagen in three different forms.

Silica-based nanoparticles have found application in the development of biocomposites involving reconstituted collagen in tissue engineering and wound healing, and leather modification, specifically targeting collagen fibers. However, a comprehensive investigation into the interaction between collagen-silica nanoparticles and different forms of collagen using biophysical methods remains unexplored. In this study, we examined the interaction between silica (SiO) nanoparticles and collagen in its fiber, microfibril, and monomer forms through high-resolution scanning electron microscopy, circular dichroism, Fourier-transform infrared spectroscopy, fluorescence analysis, zeta potential measurements, and turbidity assays.

A Novel Surfactant with Short Hydrophobic Head and Long Hydrophilic Tail Generates Vesicles with Unique Structural Feature.

Surfactant molecules typically have a long hydrophobic tail and a short hydrophilic head group. It remains unexplored if surfactants can have a short hydrophobic head group and a long hydrophilic tail. Designing such surfactants is a challenge as a lengthy hydrophilic tail would completely solubilize the molecules.

Recombinant and genetic code expanded collagen-like protein as a tailorable biomaterial.

Collagen occurs in nature with a dedicated triple helix structure and is the most preferred biomaterial in commercialized medical products. However, concerns on purity, disease transmission, and the reproducibility of animal derived collagen restrict its applications and warrants alternate recombinant sources. The expression of recombinant collagen in different prokaryotic and eukaryotic hosts has been reported with varying degrees of success, however, it is vital to elucidate the structural and biological characteristics of natural collagen.