The influence of residual water on the secondary structure and crystallinity of freeze-dried fibrinogen

Wahl, Verena; Scheibelhofer, Otto; Roessl, Ulrich; Leitgeb, Stefan; Beer, Thomas De; Khinast, Johannes G.

doi:10.1016/j.ijpharm.2015.02.010

Cited by 7 publications

(2 citation statements)

References 45 publications

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“…The band at around 1240 cm −1 was ascribed as a marker for β-conformation observed in other proteins and polypeptides [29]. In the study by Khinast et al the peaks in the region of 1230-1245 cm −1 were ascribed to β-sheet, whereas the peaks in the region of 1245-1255 cm −1 were characteristic of random coil [39]. Combining the investigations on CD spectroscopy above and the analysis on the amide I band, we speculated that a certain content of ordered secondary structures in +2SAP (such as α-helix and β-sheet) was transformed to random coil with increasing amount of lysines inserted in the designer SAPs.…”

Section: Structure Measurement By Raman Spectroscopymentioning

confidence: 96%

“…The amide III band at 1236 cm −1 in −4SAP shifted to 1242 cm −1 in −4VSAP, which was in the region of random coil and β-turn. Meanwhile, a new band assigned to α-helix structure appeared at 1276 cm −1 in the Raman spectrum of −4VSAP [39]. It has been well-documented that functional motif sequences affect the self-assembly process of the functional peptides [9,10,16].…”

Section: Structure Measurement By Raman Spectroscopymentioning

confidence: 97%

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The effects of motif net charge and amphiphilicity on the self-assembly of functionally designer RADA16-I peptides

Wu¹,

Zhang²,

Zhao³

et al. 2018

Biomed. Mater.

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RADA16-I (Ac-(RADA)-CONH) is a widely investigated self-assembling peptide (SAP) in the biomedical field. It can undergo ordered self-assembly to form stable secondary structures, thereby further forming a nanofiber hydrogel. The modification of RADA16-I with functional peptide motifs has become a popular research topic. Researchers aim to exhibit particular biomedical signaling, and subsequently, further expand its applications. However, only a few fundamental reports are available on the influences of the peptide motifs on self-assembly mechanisms of designer functional RADA16-I SAPs. In this study, we designed RGD-modified RADA16-I SAPs with a series of net charges and amphiphilicities. The assembly/reassembly of these functionally designer SAPs was thoroughly studied using Raman spectroscopy, CD spectroscopy, and AFM. The nanofiber morphology and the secondary structure largely depended on the balance between the hydrophobic effects versus like-charge repulsions of the motifs, which should be to the focus in order to achieve a tailored nanostructure. Our study would contribute insight into considerations for sophisticated design of SAPs for biomedical applications.

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Section: Structure Measurement By Raman Spectroscopymentioning

confidence: 96%