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1.
Biomacromolecules ; 18(8): 2529-2538, 2017 Aug 14.
Article in English | MEDLINE | ID: mdl-28699748

ABSTRACT

In order to prevent hemorrhage during surgical procedures, a wide range of hemostatic agents have been developed. However, their efficacy is variable; hemostatic devices that use bioactive components to accelerate coagulation are dependent on natural sources, which limits reproducibility. Hybrid devices in which chain-end reactive poly(ethylene glycol) is employed as active component sometimes suffer from irregular cross-linking and dissolution of the polar PEG when blood flow is substantial. Herein, we describe a synthetic, nonbioactive hemostatic product by coating N-hydroxysuccinimide ester (NHS)-functional poly(2-oxazoline)s (POx-NHS) onto gelatin patches, which acts by formation of covalent cross-links between polymer, host blood proteins, gelatin and tissue to seal the wound site and prevent hemorrhage during surgery. We studied different process parameters (including polymer, carrier, and coating technique) in direct comparison with clinical products (Hemopatch and Tachosil) to obtain deeper understanding of this class of hemostatic products. In this work, we successfully prove the hemostatic efficacy of POx-NHS as polymer powders and coated patches both in vitro and in vivo against Hemopatch and Tachosil, demonstrating that POx-NHS are excellent candidate polymers for the development of next generation hemostatic patches.


Subject(s)
Blood Loss, Surgical/prevention & control , Gelatin , Hemostatics , Oxazoles , Animals , Gelatin/chemistry , Gelatin/pharmacology , Hemostatics/chemistry , Hemostatics/pharmacology , Oxazoles/chemistry , Oxazoles/pharmacology , Polyethylene Glycols/chemistry , Polyethylene Glycols/pharmacology , Succinimides/chemistry , Swine
2.
Biochim Biophys Acta ; 1818(9): 2171-4, 2012 Sep.
Article in English | MEDLINE | ID: mdl-22525599

ABSTRACT

In order to enhance the membrane disruption of antimicrobial peptides both targeting and multivalent presentation approaches were explored. The antimicrobial peptides anoplin and temporin L were conjugated via click chemistry to vancomycin and to di- and tetravalent dendrimers. The vancomycin unit led to enhanced membrane disruption of large unilamellar vesicles (LUVs) displaying the vancomycin target lipid II, but only for temporin L and not for anoplin. The multivalent presentation led to enhanced LUV membrane disruption in the case of anoplin but not for temporin L.


Subject(s)
Antimicrobial Cationic Peptides/chemistry , Lipids/chemistry , Proteins/chemical synthesis , Wasp Venoms/chemical synthesis , Antimicrobial Cationic Peptides/chemical synthesis , Biophysics/methods , Chromatography, High Pressure Liquid/methods , Drug Design , Fluoresceins/chemistry , Humans , Models, Chemical , Peptides/chemistry , Phosphatidylcholines/chemistry , Phosphatidylglycerols/chemistry , Proteins/chemistry , Vancomycin/chemistry , Wasp Venoms/chemistry
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