2009
DOI: 10.1021/la903932w
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Orientation Difference of Chemically Immobilized and Physically Adsorbed Biological Molecules on Polymers Detected at the Solid/Liquid Interfaces in Situ

Abstract: A surface sensitive second order nonlinear optical technique, sum frequency generation (SFG) vibrational spectroscopy, was applied to study peptide orientation on polymer surfaces, supplemented by a linear vibrational spectroscopy, attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR). Using the antimicrobial peptide Cecropin P1 as a model system, we have quantitatively demonstrated that chemically immobilized peptides on polymers adopt a more ordered orientation than less tightly bou… Show more

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Cited by 63 publications
(121 citation statements)
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“…33,34 Our optimized peptide attachment chemistry described above results in surfaces with a helical axis of 37 ± 11°with respect to the surface (Figure 4, red). We interpret this result as approximately two-thirds of the surface-bound peptides connected by two triazoles as shown in Figure 2, while approximately one-third of the surface contains peptides that are bound by only one triazole linkage.…”
Section: ■ Characterizationmentioning
confidence: 99%
“…33,34 Our optimized peptide attachment chemistry described above results in surfaces with a helical axis of 37 ± 11°with respect to the surface (Figure 4, red). We interpret this result as approximately two-thirds of the surface-bound peptides connected by two triazoles as shown in Figure 2, while approximately one-third of the surface contains peptides that are bound by only one triazole linkage.…”
Section: ■ Characterizationmentioning
confidence: 99%
“…Ye et al [170] made use of SFG with varying polarization of the light impinging onto the samples to quantitatively probe peptide orientations adsorbed on polymer surfaces coated on solid CaF 2 substrates. They used polystyrene (PS) and polystyrene maleimide (PS-MA) and the Cysteine-terminated cecropin P1 (CP1) as a probe peptide whose amide I and II bands were monitored.…”
Section: Probing Surface Functionalizationmentioning
confidence: 99%
“…SFG is also used to study the formation of -sheet aggregates from human islet amyloid polypeptide (hIAPP) on membrane surfaces [175]. Besides membrane peptides and proteins, SFG has also been used to investigate physically adsorbed and chemically immobilized peptides and proteins at liquid/air [181] or solid/liquid interfaces [57,62,63,65,[189][190][191][192].…”
Section: Sfg: a Tool For The Biological Surface And Interfacementioning
confidence: 99%