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      Effect of Gelation Temperature on the Molecular Structure and Physicochemical Properties of the Curdlan Matrix: Spectroscopic and Microscopic Analyses

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          Abstract

          In order to determine the effect of different gelation temperatures (80 °C and 90 °C) on the structural arrangements in 1,3-β- d-glucan (curdlan) matrices, spectroscopic and microscopic approaches were chosen. Attenuated total reflection Fourier transform infrared spectroscopy (ATR FT-IR) and Raman spectroscopy are well-established techniques that enable the identification of functional groups in organic molecules based on their vibration modes. X-ray photoelectron spectroscopy (XPS) is a quantitative analytical method utilized in the surface study, which provided information about the elemental and chemical composition with high surface sensitivity. Contact angle goniometer was applied to evaluate surface wettability and surface free energy of the matrices. In turn, the surface topography characterization was obtained with the use of atomic force microscopy (AFM) and scanning electron microscopy (SEM). Described techniques may facilitate the optimization, modification, and design of manufacturing processes (such as the temperature of gelation in the case of the studied 1,3-β- d-glucan) of the organic polysaccharide matrices so as to obtain biomaterials with desired characteristics and wide range of biomedical applications, e.g., entrapment of drugs or production of biomaterials for tissue regeneration. This study shows that the 1,3-β- d-glucan polymer sample gelled at 80 °C has a distinctly different structure than the matrix gelled at 90 °C.

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          Designing hydrogels for controlled drug delivery

          Hydrogel delivery systems can leverage therapeutically beneficial outcomes of drug delivery and have found clinical use. Hydrogels can provide spatial and temporal control over the release of various therapeutic agents, including small-molecule drugs, macromolecular drugs and cells. Owing to their tunable physical properties, controllable degradability and capability to protect labile drugs from degradation, hydrogels serve as a platform in which various physiochemical interactions with the encapsulated drugs control their release. In this Review, we cover multiscale mechanisms underlying the design of hydrogel drug delivery systems, focusing on physical and chemical properties of the hydrogel network and the hydrogel-drug interactions across the network, mesh, and molecular (or atomistic) scales. We discuss how different mechanisms interact and can be integrated to exert fine control in time and space over the drug presentation. We also collect experimental release data from the literature, review clinical translation to date of these systems, and present quantitative comparisons between different systems to provide guidelines for the rational design of hydrogel delivery systems.
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            Reference database of Raman spectra of biological molecules

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              Spectroscopic methods for analysis of protein secondary structure.

              Several methods for determination of the secondary structure of proteins by spectroscopic measurements are reviewed. Circular dichroism (CD) spectroscopy provides rapid determinations of protein secondary structure with dilute solutions and a way to rapidly assess conformational changes resulting from addition of ligands. Both CD and Raman spectroscopies are particularly useful for measurements over a range of temperatures. Infrared (IR) and Raman spectroscopy require only small volumes of protein solution. The frequencies of amide bands are analyzed to determine the distribution of secondary structures in proteins. NMR chemical shifts may also be used to determine the positions of secondary structure within the primary sequence of a protein. However, the chemical shifts must first be assigned to particular residues, making the technique considerably slower than the optical methods. These data, together with sophisticated molecular modeling techniques, allow for refinement of protein structural models as well as rapid assessment of conformational changes resulting from ligand binding or macromolecular interactions. A selected number of examples are given to illustrate the power of the techniques in applications of biological interest. Copyright 2000 Academic Press.
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                Author and article information

                Journal
                Int J Mol Sci
                Int J Mol Sci
                ijms
                International Journal of Molecular Sciences
                MDPI
                1422-0067
                26 August 2020
                September 2020
                : 21
                : 17
                : 6154
                Affiliations
                [1 ]Department of Biopharmacy, Medical University of Lublin, Chodzki 4a, 20-093 Lublin, Poland; barbaragieroba@ 123456umlub.pl (B.G.); grkalisz@ 123456gmail.com (G.K.)
                [2 ]Department of Genetics and Microbiology, Institute of Microbiology and Biotechnology, Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland
                [3 ]Department of Biochemistry and Biotechnology, Medical University of Lublin, Chodzki 1, 20-093 Lublin, Poland; paulina.kazimierczak@ 123456umlub.pl
                [4 ]Institute of Physical Chemistry, Polish Academy of Sciences, Kasprzaka 44/52, 01-224 Warsaw, Poland; ipieta@ 123456ichf.edu.pl (I.S.P.); rnowakowski@ 123456ichf.edu.pl (R.N.); mpisarek@ 123456ichf.edu.pl (M.P.)
                Author notes
                [* ]Correspondence: annasroka@ 123456tlen.pl or anna.sroka@ 123456umlub.pl (A.S.-B.); agata.przekora@ 123456umlub.pl (A.P.); Tel.: +48-81448-7225 (A.S.-B.); +48-81448-7026 (A.P.)
                Author information
                https://orcid.org/0000-0001-8549-9848
                https://orcid.org/0000-0002-5893-7168
                https://orcid.org/0000-0001-5159-6308
                https://orcid.org/0000-0002-3394-7116
                https://orcid.org/0000-0002-8103-3044
                https://orcid.org/0000-0002-7424-5954
                https://orcid.org/0000-0002-6076-1309
                Article
                ijms-21-06154
                10.3390/ijms21176154
                7504023
                1572da6d-dfea-44bf-bf9f-defd071397dc
                © 2020 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 14 July 2020
                : 23 August 2020
                Categories
                Article

                Molecular biology
                biopolymers,1,3-β-d-glucan,vibrational spectroscopy,x-ray photoelectron spectroscopy,afm microscopy,biomaterials

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