کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
606219 1454517 2016 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Insights into the morphology of human serum albumin and sodium dodecyl sulfate complex: A spectroscopic and microscopic approach
ترجمه فارسی عنوان
مقدمه ای بر مورفولوژی آلبومین سرم انسان و مجتمع سدیم دودسیل سولفات: رویکرد طیفی و میکروسکوپی
کلمات کلیدی
طیف سنجی فلورسانس، پیچیده پروتئین سورفکتانت، مدل گردنبند و مهره، آلبومین سرم انسان، میکروسکوپ فوتولومینسانس
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی شیمی کلوئیدی و سطحی
چکیده انگلیسی

Exploring and understanding the fundamental interaction between protein and surfactant is utmost important for various pharmaceutical and biomedical applications. However, very less is known about the arrangement of individual negatively charged sodium dodecyl sulfate (SDS) molecules on the human serum albumin (HSA). Here, we have investigated the morphology and mechanistic insights of complexation between HSA and SDS by means of photoluminescence (PL) spectroscopy, circular dichroism (CD) and PL microscopy using amine-functionalized silicon quantum dot (Si QD) as an external luminescent marker. The present study is based on a unique and dynamic SDS-Si QD system. The synthesized allylamine–functionalized Si QDs show a distinct PL band centered at 455 nm upon excitation at 375 nm. At neutral pH, these Si QDs form ordered aggregates in the presence of 1 mM SDS due to the hydrogen bonding interaction with the sulfate head groups of surfactants, which is manifested in the appearance of a large Stokes shifted luminescence band centered at 610 nm. It has been observed that the PL intensity of SDS-Si QD aggregates at 610 nm decreases gradually with concomitant increase in the PL intensity of monomeric Si QDs at 455 nm upon increasing the concentration of HSA from 1 to 10 μM. These observations combined with PL lifetime, PL microscopy and CD results reveal that SDS forms micelle-like aggregates on the partially unfolded HSA mainly via electrostatic interaction between negatively charged sulfate head groups and positively charged residues of partially unfolded HSA. For the present HSA-SDS system, our results fit a model with type I “necklace and bead”-like structures, where micelle-like SDS aggregates wrap around by the partially unfolded HSA backbone.

The morphology and mechanistic insights of complexation between human serum albumin (HSA) and sodium dodecyl sulfate (SDS) have been explored by means of photoluminescence spectroscopy, circular dichroism and PL microscopy using amine-functionalized silicon quantum dot (Si QD) as an external luminescent marker.Figure optionsDownload high-quality image (133 K)Download as PowerPoint slide

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Colloid and Interface Science - Volume 478, 15 September 2016, Pages 29–35
نویسندگان
, ,