Jonathan Anderson, Meng-Hsien Lin, Caitlyn Privette, Marissa Flowers, Meridith Murley, Bruce P Lee, Keat Ghee Ong
{"title":"Wireless magnetoelastic sensors for tracking degradation profiles of nitrodopamine-modified poly(ethylene glycol).","authors":"Jonathan Anderson, Meng-Hsien Lin, Caitlyn Privette, Marissa Flowers, Meridith Murley, Bruce P Lee, Keat Ghee Ong","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A critical property for tissue adhesives is a controllable degradation rate so that these adhesives do not act as barriers to wound healing. Typical degradation tests require large amount of samples, which can be tedious and expensive to perform. Additionally, current degradation tests are carried out <i>in vitro</i> under simulated physiological conditions and may not accurately reflect the complex environment that an adhesive would experience <i>in vivo</i>. As a means to develop a simple technique for testing tissue adhesive, a rapidly degrading adhesive hydrogel that mimics mussel adhesive proteins was coated onto magnetoelastic (ME) sensor strips to track the degradation of the adhesive remotely and in real time. Adhesive-coated ME sensors were submerged in phosphate buffer saline solution (pH 7.4) at body temperature (37 °C). Based on the change in the resonant amplitude, the degradation time was determined to be 22 min, which was in agreement with qualitative monitoring of the bulk adhesive hydrogel. Additionally, when the adhesive-coated ME sensor was incubated in a slightly acidic medium (pH 5.7), the degradation rate was drastically lengthened (3 hrs) as the hydrolysis of ester bonds is faster under basic conditions. Oscillatory rheological testing confirmed the formation and degradation of the adhesive. However, rheological test results did not accurately reflect the degradation rate of the adhesive hydrogel, potentially due to a slow exchange of acidic degradation products with the surrounding medium. ME sensor was demonstrated as a potential useful tool for evaluating the degradation rate of bioadhesives.</p>","PeriodicalId":90724,"journal":{"name":"Sciencejet","volume":"4 80","pages":""},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4335653/pdf/nihms662411.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33079574","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Sabarinathan K Gopalasubramaniam, Kalyan C Kondapalli, César Millán-Pacheco, Nina Pastor, Timothy L Stemmler, Jose F Moran, Raúl Arredondo-Peter
{"title":"Soybean dihydrolipoamide dehydrogenase (ferric leghemoglobin reductase 2) interacts with and reduces ferric rice non-symbiotic hemoglobin 1.","authors":"Sabarinathan K Gopalasubramaniam, Kalyan C Kondapalli, César Millán-Pacheco, Nina Pastor, Timothy L Stemmler, Jose F Moran, Raúl Arredondo-Peter","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Ferrous oxygenated hemoglobins (Hb<sup>2+</sup>O<sub>2</sub>) autoxidize to ferric Hb<sup>3+</sup>, but Hb<sup>3+</sup> is reduced to Hb<sup>2+</sup> by enzymatic and non-enzymatic mechanisms. We characterized the interaction between the soybean ferric leghemoglobin reductase 2 (FLbR2) and ferric rice non-symbiotic Hb1 (Hb1<sup>3+</sup>). Spectroscopic analysis showed that FLbR2 reduces Hb1<sup>3+</sup>. Analysis by tryptophan fluorescence quenching showed that FLbR2 interacts with Hb1<sup>3+</sup>, however the use of ITC and IEF techniques revealed that this interaction is weak. <i>In silico</i> modeling showed that predicted FLbR2 and native Hb1<sup>3+</sup> interact at the FAD-binding domain of FLbR2 and the CD-loop and helix F of Hb1<sup>3+</sup>.</p>","PeriodicalId":90724,"journal":{"name":"Sciencejet","volume":"2 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4243682/pdf/nihms601276.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32843652","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}