Kjellström S
Bioactive Suture with Added Innate Defense Functionality for the Reduction of Bacterial Infection and Inflammation.
Of more than 300 million surgical procedures performed worldwide annually,[1] almost 10% develop surgical site infections (SSIs).[2] SSIs account for a substantial clinical and economic burden.[3] Although many factors contribute to SSIs, preventive measures before, during, and after surgery can lower the SSI incidence.[4] Causes of SSIs vary depending on anatomy, surgical procedure, and exogenous in addition to endogenous, patient-derived factors. Bacterial contamination is one cause that can be controlled.[4, 5] In hospitals, preventive measures such as hygiene routines are implemented but even under sterile surgical conditions, infections may occur due to the spread of bacteria from the patient's own bacterial flora.[6] It has also been reported that up to 60% of the bacteria recovered from infected surgical wounds developed antibiotic resistance.[7]
ReadTargeting Toll-like receptor-driven systemic inflammation by engineering an innate structural fold into drugs.
There is a clinical need for conceptually new treatments that target the excessive activation of inflammatory pathways during systemic infection.
ReadObservation of multiple protein temperature transitions dependent upon the chemical environment
Surgical site infections (SSI) are a clinical and economic burden. Suture-associated SSI may develop when bacteria colonize the suture surface and form biofilms that are resistant to antibiotics.
ReadStructural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptides
Thrombin-derived C-terminal peptides (TCPs) of about 2 kDa are present in wounds, where they exert anti-endotoxic functions. Employing a combination of nuclear magnetic resonance spectroscopy (NMR), biophysical, mass spectrometry and cellular studies combined with in silico multiscale modelling, we here determine the bound conformation of HVF18 (HVFRLKKWIQKVIDQFGE), a TCP generated by neutrophil elastase, in complex with bacterial lipopolysaccharide (LPS) and define a previously undisclosed interaction between TCPs and human CD14.
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