The assembly state and charge of amphiphilic β-sheet peptides affect blood clotting

Azoulay, Ziv; Rapaport, Hanna

doi:10.1039/c6tb00330c

Cited by 19 publications

(20 citation statements)

References 37 publications

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“…The capacity of blood to clot upon contact with AMP-hydrogels can be explained by the interaction of positively charged AMPs with blood cells, platelets, and plasma fibronectin to induce hemostasis. Furthermore, the capability of hydrogels to absorb blood facilitated the interaction of blood cells with AMPs to induce blood clotting. , The results suggest that using AMP-hydrogel as a wound patch can accelerate blood coagulation and clot formation for a bleeding wound. That can be considered as a desirable additional property provided by AMP-hydrogels apart from the antibacterial effect.…”

Section: Resultsmentioning

confidence: 89%

“…Furthermore, the capability of hydrogels to absorb blood facilitated the interaction of blood cells with AMPs to induce blood clotting. 49,50 The results suggest that using AMPhydrogel as a wound patch can accelerate blood coagulation and clot formation for a bleeding wound. That can be considered as a desirable additional property provided by AMP-hydrogels apart from the antibacterial effect.…”

Section: ■ Results and Discussionmentioning

confidence: 96%

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Antimicrobial Peptide-Functionalized Mesoporous Hydrogels

Atefyekta

Blomstrand

Rajasekharan

et al. 2021

ACS Biomater. Sci. Eng.

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Antimicrobial peptides (AMPs) are seen as a promising replacement to conventional antibiotics for the prevention of skin wound infections. However, due to the short half-life of AMPs in biological environments, such as blood, their use in clinical applications has been limited. The covalent immobilization of AMPs onto suitable substrates is an effective solution to create contact-killing surfaces with increased long-term stability. In this work, an antimicrobial peptide, RRPRPRPRPWWWW-NH2 (RRP9W4N), was covalently attached to amphiphilic and ordered mesoporous Pluronic F127 hydrogels made of cross-linked lyotropic liquid crystals through 1-ethyl-3-(3-(dimethylamino)propyl) carbodiimide (EDC) and N -hydroxysuccinimide (NHS) chemistry. The AMP-hydrogels showed high antibacterial activity against Staphylococcus epidermidis, Staphylococcus aureus , Pseudomonas aeruginosa , methicillin-resistant S. aureus (MRSA), and multidrug-resistant Escherichia coli for up to 24 h. Furthermore, the AMP-hydrogels did not present any toxicity to human fibroblasts. The AMPs retained their antimicrobial activity up to 48 h in human blood serum, which is a significant increase in stability compared to when used in dissolved state. A pilot in vivo rat model showed 10–100× less viable counts of S. aureus on AMP-hydrogels compared with control hydrogels during the first 3 days of infection. Studies performed on human whole blood showed that blood coagulated more readily in the presence of AMP-hydrogels as compared to hydrogels without AMPs, indicating potential hemostatic activity. Overall, the results suggest that the combination of amphiphilic hydrogels with covalently bonded AMPs has potential to be used as antibacterial wound dressing material to reduce infections and promote hemostatic activity as an alternative to antibiotics or other antimicrobial agents, whose use should be restricted.

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Section: Resultsmentioning

confidence: 89%

Section: ■ Results and Discussionmentioning

confidence: 96%

Antimicrobial Peptide-Functionalized Mesoporous Hydrogels

Atefyekta

Blomstrand

Rajasekharan

et al. 2021

ACS Biomater. Sci. Eng.

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“…On the other hand, the positivecharged peptide could induce hemostasis through electrostatic attraction to adhere blood cells, platelets, and plasma fibronectin. 48 2.7. In Vivo Hemostatic Properties of the Hydrogels.…”

Section: Resultsmentioning

confidence: 99%

Peptide-Functionalized Amino Acid-Derived Pseudoprotein-Based Hydrogel with Hemorrhage Control and Antibacterial Activity for Wound Healing

et al. 2019

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Developing permanent antibacterial and rapid hemostatic wound dressings with excellent biocompatibility is urgently needed and has always gained great attention. Here, a series of amino acid-derived pseudoprotein consisting of poly(ester amide) (PEA)-based hydrogel dressings and three types of cationic short peptides (RGDK, RRRFK, and RRRFRGDK) are prepared. Compared with the antibacterial segments containing hydrogel scaffolds, the method of peptide modification of surface possesses the minimal usage of antibacterial moiety due to the effective contacting wound spots. Direct peptide RRRFRGDK (P3) conjugation to the hydrogel surface through an amidization reaction can enhance the antibacterial and hemostatic abilities with no or minimal outer appearance and inner morphology damage to the original hydrogels. The P3-functionalized hydrogel (Gel-g-P3) presents excellent water uptake capacity, robust mechanical strength, enzymatic biodegradation, good hemocompatibility, and cytocompatibility. Moreover, the Gel-g-P3 hydrogel has better adhesion capacities of blood cell and platelet and exhibits shorter hemostasis time in the mouse-liver injury model. Finally, the wound healing performance is evaluated in vivo using an infected wound model. The results show that the Gel-g-P3 hydrogel has accelerated the wound healing process, implying that the peptide-functionalized PEA-based hydrogels can be used as hemostasis agents and wound dressings for infected wounds.

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“…For example, a high percentage of hydrophobic (aliphatic and aromatic) AA residues in antidiabetic peptides (Figure 4) [109][110][111] is necessary for inhibition of dipeptidyl peptidase IV, a key enzyme involved in degradation of incretins [110,112,113], and for recognition of receptors for glucagon-like peptides [114,115]. A high percentage of negatively charged AA residues (Figure 4) has been reported in antithrombotic peptides showing both direct thrombin inhibition [116,117] and inhibition of factors in intrinsic pathways [72,118]. A high frequency of positively charged AA residues in so-called cationic antimicrobial peptides ( Figure 4) [119][120][121] is proven to be necessary for interactions with anionic microbe membranes.…”

Section: Comparison Of the Structures Of Marine-sourced Peptides Withmentioning

confidence: 99%

Marine Bioactive Peptides—An Overview of Generation, Structure and Application with a Focus on Food Sources

2020

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The biggest obstacles in the application of marine peptides are two-fold, as in the case of non-marine plant and animal-derived bioactive peptides: elucidating correlation between the peptide structure and its effect and demonstrating its stability in vivo. The structures of marine bioactive peptides are highly variable and complex and dependent on the sources from which they are isolated. They can be cyclical, in the form of depsipeptides, and often contain secondary structures. Because of steric factors, marine-derived peptides can be resistant to proteolysis by gastrointestinal proteases, which presents an advantage over other peptide sources. Because of heterogeneity, amino acid sequences as well as preferred mechanisms of peptides showing specific bioactivities differ compared to their animal-derived counterparts. This review offers insights on the extreme diversity of bioactivities, effects, and structural features, analyzing 253 peptides, mainly from marine food sources. Similar to peptides in food of non-marine animal origin, a significant percentage (52.7%) of the examined sequences contain one or more proline residues, implying that proline might play a significant role in the stability of bioactive peptides. Additional problems with analyzing marine-derived bioactive peptides include their accessibility, extraction, and purification; this review considers the challenges and proposes possible solutions.

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The assembly state and charge of amphiphilic β-sheet peptides affect blood clotting

Abstract: Hydrogels composed of designed β-sheet amphiphilic peptides have been exploited in several biomedical applications. Here the peptide's charge shows influence on blood compatibility with antithrombotic or no effects on clotting blood given by the anionic and zwitterionic peptides.

Cited by 19 publications

References 37 publications

Antimicrobial Peptide-Functionalized Mesoporous Hydrogels

Antimicrobial Peptide-Functionalized Mesoporous Hydrogels

Peptide-Functionalized Amino Acid-Derived Pseudoprotein-Based Hydrogel with Hemorrhage Control and Antibacterial Activity for Wound Healing

Marine Bioactive Peptides—An Overview of Generation, Structure and Application with a Focus on Food Sources

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