Direct Observation of Antifreeze Glycoprotein-Fraction 8 on Hydrophobic and Hydrophilic Interfaces Using Atomic Force Microscopy

Sarno, David M.; Murphy, Anastasia V.; Divirgilio, Evan S.; Jones, Wayne E.; Ben, Robert N.

doi:10.1021/la027046l

Cited by 16 publications

(21 citation statements)

References 20 publications

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“…In our experiment, we rinsed the deposits of the AFGP solutions three times using distilled water, as reported in Ref. 6. The peak positions in the I region remained the same and their intensities decreased only insignificantly compared with those from samples without rinsing.…”

Section: Resultsmentioning

confidence: 73%

“…AFM experiments in the Ref. 6 have demonstrated that the AFGP 8 covered the nanometer-size steps edges and planes in the HOPG surface. In the step regions, the facets of the HOPG can be different from the c face or the (0001) plane.…”

Section: Resultsmentioning

confidence: 99%

“…4 To characterize the adsorption process, Lavalle et al 5 have studied mixtures of AFGPs 1, 2, 3, 4 and 5 on two silicate minerals using atomic force microscopy (AFM) and optical waveguide lightmode spectroscopic techniques. More recently, Sarno et al 6 have studied the adsorption of AFGP 8 on hydrophobic HOPG and hydrophilic mica surfaces using AFM and molecular dynamical simulation. These authors have shown that preferential adsorption occurred at the hydrophilic step edges, with homogeneous aggregation of AFGP 8 on hydrophobic planes.…”

Section: Introductionmentioning

confidence: 99%

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Raman spectroscopy shows antifreeze glycoproteins interact with highly oriented pyrolytic graphite

Cui

Turner

Roy

et al. 2005

J Raman Spectroscopy

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Raman spectra of a mixture of antifreeze glycoproteins (AFGP) 6, 7 and 8 adsorbed on a highly oriented pyrolytic graphite (HOPG) surface spanning the range of 50 to 4500 cm −1 were measured. It was found that the Raman signature of AFGP had been significantly altered because of its interaction with the HOPG surface; when compared with the spectra of bulk AFGP compounds, at least three new peaks were observed around 860, 940 and 1000 cm −1 , and two other peaks that were not well resolved in the bulk spectra around 1050 and 1155 cm −1 were enhanced and well discriminated. The peak positions depended on the facet of HOPG presented to the proteins, and their relative intensities depended on the concentration of AFGP used in the adsorption experiment. The results indicated the possibility of multiple binding sites of AFGP on HOPG surfaces.

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Section: Resultsmentioning

confidence: 73%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Raman spectroscopy shows antifreeze glycoproteins interact with highly oriented pyrolytic graphite

Cui

Turner

Roy

et al. 2005

J Raman Spectroscopy

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show abstract

“…[70] The results showed that AFGP8 binds preferentially to the hydrophilic step edges of the surface. It was further shown that AFGP8 deposited on mica by the solution droplet evaporation technique resulted in patterned surfaces formed by a single layer of protein, [71] and that AFGP aggregates prior to deposition.…”

Section: Surface Studiesmentioning

confidence: 96%

Design and Synthesis of Antifreeze Glycoproteins and Mimics

Harding

2010

ChemBioChem

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Antifreeze glycoproteins are an important class of biological antifreezes that have potential applications in many areas of medicine, agriculture and industry in which ice crystal growth is damaging. While the synthesis of antifreeze glycoproteins as pure glycoforms has recently been achieved by using ligation and polymerisation strategies, the routine production of large quantities of pure glycoforms remains challenging. A range of C-linked analogues that are readily produced by solid-phase synthesis have delivered novel compounds that are not biological antifreezes, but are potent, non-cytotoxic, ice-recrystallisation inhibitors. Structure-activity studies, the identification of cyclic antifreeze glycoproteins and conformational studies have provided further insight into the requirements for antifreeze activity. These results, coupled with significant advances in approaches to the routine synthesis of different glycoproteins and mimics, present opportunities for the design and synthesis of novel ice-growth-inhibiting and antifreeze compounds.

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“…Recently, the interaction 0927-7765/$ -see front matter © 2010 Elsevier B.V. All rights reserved. doi:10.1016/j.colsurfb.2010.08.029 of antifreeze proteins with hydrophilic and hydrophobic surfaces, such as mica and graphite, has been explored with the hope of gaining insight into the nature of these peptide-surface interactions [29][30][31][32]. The results showed that binding to hydrophilic mica takes place over the entire surface due to its hydrophilic nature, but the adsorption of AFGPs to graphite was different.…”

Section: Introductionmentioning

confidence: 99%