Infrared study of gelatin conformations in the gel and sol states

Prystupa, D. A.; Donald, Athene M.

doi:10.1016/0966-7822(96)00003-2

Cited by 160 publications

(100 citation statements)

References 40 publications

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“…The wavenumber of the characteristic band of these carbonyl groups is determined by the local chemical environment and the degree of dipole-dipole interaction between neighboring carbonyl groups [42]. The band at 1,664 cm −1 is related to the presence of both triple helices and β-turns [42]. The amide II region consists of a band at 1,556 cm −1 (i.e., NH bend coupled with CN stretch) [43].…”

Section: Pimentioning

confidence: 99%

“…The amide I band, which is due primarily to C=O stretching of the peptide groups, is extremely sensitive to changes in the gelatin chain conformation. The wavenumber of the characteristic band of these carbonyl groups is determined by the local chemical environment and the degree of dipole-dipole interaction between neighboring carbonyl groups [42]. The band at 1,664 cm −1 is related to the presence of both triple helices and β-turns [42].…”

Section: Pimentioning

confidence: 99%

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Gelatin Functionalization of Biomaterial Surfaces: Strategies for Immobilization and Visualization

et al. 2011

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Abstract:In the present work, the immobilization of gelatin as biopolymer on two types of implantable biomaterials, polyimide and titanium, was compared. Both materials are known for their biocompatibility while lacking cell-interactive behavior. For both materials, a pre-functionalization step was required to enable gelatin immobilization. For the polyimide foils, a reactive succinimidyl ester was introduced first on the surface, followed by covalent grafting of gelatin. For the titanium material, methacrylate groups were first introduced on the Ti surface through a silanization reaction. The applied functionalities enabled the subsequent immobilization of methacrylamide modified gelatin. Both surface modified materials were characterized in depth using atomic force microscopy, static contact angle measurements, confocal fluorescence microscopy, attenuated total reflection infrared spectroscopy and X-ray photo-electron spectroscopy. The results indicated that the strategies elaborated for both material classes are suitable to apply stable gelatin coatings. Interestingly, depending on the material class studied, not all surface analysis techniques are applicable.

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Section: Pimentioning

confidence: 99%

Section: Pimentioning

confidence: 99%

Gelatin Functionalization of Biomaterial Surfaces: Strategies for Immobilization and Visualization

et al. 2011

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“…In a collagen-unfold structure, the aligned α-helical domain is divided into single chains, which suggests that the regenerative β-sheet is the intermediate instead of single chains and is very unstable [16,28]. As a consequence, the partial β-sheet bands in ICFs disappeared during the cooling, which indicate a partial reverse of the collagen-fold structures [16]. However, ICFs and PSCs showed some differences.…”

Section: D Correlation Analysis Of Icfs and Pscsmentioning

confidence: 94%

“…These results agree well with previous research [28,29], indicating the collagen-unfold structures were formed during the heating process. In a collagen-unfold structure, the aligned α-helical domain is divided into single chains, which suggests that the regenerative β-sheet is the intermediate instead of single chains and is very unstable [16,28]. As a consequence, the partial β-sheet bands in ICFs disappeared during the cooling, which indicate a partial reverse of the collagen-fold structures [16].…”

Section: D Correlation Analysis Of Icfs and Pscsmentioning

confidence: 94%

“…The spectral changes detected by the FSD analyses were in agreement with those observed by the second derivative analysis. Prystupa and Donald [16] reported that the spectra obtained from D2O solutions were of better quality than those obtained for H2O solutions. Figure 3 shows the amide I region in the FSD spectra of ICFs and PSCs dispersed in D2O (5% w/v) at 5 °C.…”

Section: Ftir Spectra Of Icfs and Pscsmentioning

confidence: 98%

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Unfolding/Refolding Study on Collagen from Sea Cucumber Based on 2D Fourier Transform Infrared Spectroscopy

Qin

et al. 2016

Molecules

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Abstract:We aimed to explore the differences of thermal behaviors between insoluble collagen fibrils (ICFs) and pepsin-solubilized collagens (PSCs) from sea cucumber Stichopus japonicus. The unfolding/refolding sequences of secondary structures of ICFs and PSCs during the heating and cooling cycle (5 → 70 → 5 • C) were identified by Fourier transform infrared spectrometry combined with curve-fitting and 2D correlation techniques. ICFs showed a higher proportion of α-helical structures and higher thermostability than PSCs, and thus had more-stable triple helical structures. The sequences of changes affecting the secondary structures during heating were essentially the same between ICFs and PSCs. In all cases, α-helix structure was the most important conformation and it disappeared to form a β-sheet structure. In the cooling cycle, ICFs showed a partially refolding ability, and the proportion of β-sheet structure rose before the increasing proportion of α-helix structure. PSCs did not obviously refold during the cooling stage.

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Processing and Industrial Aspects of Fish‐scale Collagen: A Biomaterials Perspective

Dhara

Datta

Pal

et al. 2013

Marine Proteins and Peptides

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Infrared study of gelatin conformations in the gel and sol states

Cited by 160 publications

References 40 publications

Gelatin Functionalization of Biomaterial Surfaces: Strategies for Immobilization and Visualization

Gelatin Functionalization of Biomaterial Surfaces: Strategies for Immobilization and Visualization

Unfolding/Refolding Study on Collagen from Sea Cucumber Based on 2D Fourier Transform Infrared Spectroscopy

Processing and Industrial Aspects of Fish‐scale Collagen: A Biomaterials Perspective

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