A multiphase transitioning peptide hydrogel for suturing ultrasmall vessels

Smith, Daniel J.; Brat, Gabriel; Medina, Scott H.; Tong, Dedi; Huang, Yong; Grahammer, Johanna; Furtmüller, Georg J.; Oh, Byoung Chol; Nagy-Smith, Katelyn; Walczak, Piotr; Brandacher, Gerald; Schneider, Joel P.

doi:10.1038/nnano.2015.238

Cited by 142 publications

(93 citation statements)

References 27 publications

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“…The development of biomaterials derived from self‐assembled peptides is of great current interest due to biomedical applications including controlled release drug delivery, vaccine development, tissue engineering, and wound healing . Amphipathic peptides that consist of alternating hydrophobic and hydrophilic amino acids are a privileged class of peptide that readily self‐assembles into β‐sheet bilayer nanoribbons that share the basic characteristics of cross‐β amyloid assemblies (Figure ) .…”

Section: Introductionmentioning

confidence: 99%

Balancing hydrophobicity and sequence pattern to influence self‐assembly of amphipathic peptides

2018

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Amphipathic peptides with alternating polar and nonpolar amino acid sequences efficiently selfassemble into functional b-sheet fibrils as long as the nonpolar residues have sufficient hydrophobicity. For example, the Ac-(FKFE) 2 -NH 2 peptide rapidly self-assembles into b-sheet bilayer nanoribbons, while Ac-(AKAE) 2 -NH 2 fails to self-assemble under similar conditions due to the significantly reduced hydrophobicity and b-sheet propensity of Ala relative to Phe. Herein, we systematically explore the effect of substituting only two of the four Ala residues at various positions in the Ac-(AKAE) 2 -NH 2 peptide with amino acids of increasing hydrophobicity, b-sheet potential, and surface area (including Phe, 1-naphthylalanine (1-Nal), 2-naphthylalanine (2-Nal), cyclohexylalanine (Cha), and pentafluorophenylalanine (F 5 -Phe)) on the self-assembly propensity of the resulting sequences. It was found that double Phe variants, regardless of the position of substitution, failed to self-assemble under the conditions used in this study. In contrast, all double 1-Nal and 2-Nal variants readily self-assembled, albeit at differing rates depending on the substitution patterns. To determine whether this was due to hydrophobicity or side chain surface area, we also prepared double Cha and F 5 -Phe variant peptides (both side chain groups are more hydrophobic than Phe). Each of these variants also underwent effective self-assembly, with the aromatic F 5 -Phe peptides doing so with greater efficiency. These findings provide insight into the role of amino acid hydrophobicity and sequence pattern on self-assembly proclivity of amphipathic peptides and on how targeted substitutions of nonpolar residues in these sequences can be exploited to tune the characteristics of the resulting self-assembled materials.hydrophobicity, peptide, self-assembly | I N TR ODU C TI ONThe development of biomaterials derived from self-assembled peptides is of great current interest due to biomedical applications including controlled release drug delivery, vaccine development, tissue engineering, and wound healing. Amphipathic peptides that consist of alternating hydrophobic and hydrophilic amino acids are a privileged class of peptide that readily self-assembles into b-sheet bilayer nanoribbons that share the basic characteristics of cross-b amyloid assemblies (Figure 1). [23][24][25][26][27][28][29][30] These bilayer nanoribbons effectively sequester all hydrophobic functionality to the bilayer interior, leaving hydrophilic groups exposed to solvent on the exterior face. [24,[31][32][33][34] As a result, these nanoribbons maintain high solubility in aqueous solvents, making them ideal materials for biological applications. Because of the high utility of this class of amphipathic peptide, they have been widely adopted as models to study the fundamental physicochemical basis of peptide self-assembly processes in order to facilitate the rational design of next-generation materials derived from self-assembled b-sheet peptides.[ [35][36][37][38][39]...

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Section: Introductionmentioning

confidence: 99%

Balancing hydrophobicity and sequence pattern to influence self‐assembly of amphipathic peptides

2018

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“…[2] In addition, tissue adhesive can be utilized quickly and easily at irregular sites, and minimizes inflammatory or immune reactions. [1] However, strategies to improve adhesive quality and the demand for new adhesives require continuous development to overcome the disadvantages of currently used commercial adhesives and fulfill all the requirements of clinical use, such as facile operation, biocompatible and degradable materials, biological integration, and strong tissue-tissue or tissueimplant attachment.…”

Section: Introductionmentioning

confidence: 99%

Enhanced tissue adhesiveness of injectable gelatin hydrogels through dual catalytic activity of horseradish peroxidase

et al. 2017

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Development of bioadhesives with tunable mechanical strength, high adhesiveness, biocompatibility, and injectability is greatly desirable in all surgeries to replace or complement the sutures and staples. Herein, the dual catalytic activity of horseradish peroxidase is exploited to in situ form the hydroxyphenyl propionic acid-gelatin/thiolated gelatin (GH/GS) adhesive hydrogels including two alternative crosslinks (phenol-phenol and disulfide bonds) with fast gelation (few seconds -several minutes) and improved physicochemical properties. Their elastic moduli increase from 6.7 to 10.3 kPa by adding GS polymer that leads to the better stability of GH/GS hydrogels than GH ones.GH/GS adhesive strength is respectively 6.5-fold and 15.8-fold higher than GH-only and fibrin glue that is due to additional disulfide linkages between hydrogels and tissues. Moreover, in vitro cell study with human dermal fibroblast showed the cell-compatibility of GH/GS hydrogels. Taken together, GH/GS hydrogels can be considered as promising potential adhesive materials for various biomedical applications. K E Y W O R D Sadhesives, biodegradability, gelatin, in situ forming hydrogels, thiomers

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“…Therefore, biomaterials acting as an artificial microenvironment for guiding cells must mimic the functions of glycoproteins and phosphoproteins. [8] But the synthesis of glycans remains a daunting challenge, [9] and the controlled protein phosphorylation is hardly an easy task. Thus, it is imperative to develop a facile approach for generating next generation biomaterials that mimic the functions of extracellular glycoproteins and phosphoproteins.…”

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confidence: 99%

An in situ Dynamic Continuum of Supramolecular Phosphoglycopeptides Enables Formation of 3D Cell Spheroids

et al. 2017

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Higher-order assemblies of proteins, with a structural and dynamic continuum, is an important concept in biology, but these insights have yet to be applied in designing biomaterials. Dynamic assemblies of supramolecular phosphoglycopeptides (sPGPs) transform a 2D cell sheet into 3D cell spheroids. A ligand-receptor interaction between a glycopeptide and a phosphopeptide produces sPGPs that form nanoparticles, which transform into nanofibrils upon partial enzymatic dephosphorylation. The assemblies form dynamically and hierarchically in situ on the cell surface, and interact with the extracellular matrix molecules and effectively abolish contact inhibition of locomotion (CIL) of the cells. Integrating molecular recognition, catalysis, and assembly, these active assemblies act as a dynamic continuum to disrupt CIL, thus illustrating a new kind of biomaterial for regulating cell behavior.

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A multiphase transitioning peptide hydrogel for suturing ultrasmall vessels

Cited by 142 publications

References 27 publications

Balancing hydrophobicity and sequence pattern to influence self‐assembly of amphipathic peptides

Balancing hydrophobicity and sequence pattern to influence self‐assembly of amphipathic peptides

Enhanced tissue adhesiveness of injectable gelatin hydrogels through dual catalytic activity of horseradish peroxidase

An in situ Dynamic Continuum of Supramolecular Phosphoglycopeptides Enables Formation of 3D Cell Spheroids

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