Human Growth Hormone Adsorption Kinetics and Conformation on Self-Assembled Monolayers

Buijs, Jos; Britt, David W.; Hlady, Vladimir

doi:10.1021/la970669s

Cited by 48 publications

(34 citation statements)

References 26 publications

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“…The contact angles of the OTS and EDA surfaces are in good agreement with literature values [14,16]. The contact angles attained for the phospholipid headgroups, however, are rather high, a possible result from monolayer rearrangement in the presence of the captive air bubble [13]. The higher contact angle for cationic Et-DPPC monolayers versus the DPPS and DPPC monolayers is attributed to a less dense packing due to steric hindrance and charge repulsion.…”

Section: Fluorescence and Scanning Force Microscopy (Sfm)supporting

confidence: 88%

“…In a recent study we demonstrated that LB films with greater mobility adsorbed less human growth hormone than surfaces of similar chemistry but decreased mobility [13]. We attributed this effect to an unfavorable loss of surface conformational entropy upon protein adsorption.…”

Section: Sfm Imaging Of Adsorbed Tmvmentioning

confidence: 79%

“…Octadecyltrichlorosilane (OTS) and LB films were prepared on fused silica as previously described [12,13]. Silica slides were aminated using N-(2-aminoethyl)(3-aminopropyl)trimethoxysilane (EDA) according to the method of Stenger et al [14] and stored under nitrogen until use.…”

Section: Surface Preparation and Characterizationmentioning

confidence: 99%

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Tobacco mosaic virus adsorption on self-assembled and Langmuir–Blodgett monolayers studied by TIRF and SFM

1998

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The adsorption of tobacco mosaic virus (TMV) on self-assembled and Langmuir-Blodgett monolayers was investigated using total internal reflection fluorescence (TIRF) spectroscopy and scanning force microscopy (SFM). Substrates were chosen to probe electrostatic, hydrophobic and surface fluidity effects on TMV adsorption. Positively charged and hydrophobic surfaces demonstrated similar initial rates of TMV adsorption; however, their respective surface TMV coverages differed greatly. Likewise, positively charged surfaces which differed primarily in surface fluidity exhibited similar adsorption rates for TMV, but different TMV surface coverages. In contrast, virus adsorption to negatively charged and zwitterionic substrates was negligible. To elucidate these differences in adsorption behavior, SFM was used to image the distribution and the aggregation state of adsorbed TMV.

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Section: Fluorescence and Scanning Force Microscopy (Sfm)supporting

confidence: 88%

Section: Sfm Imaging Of Adsorbed Tmvmentioning

confidence: 79%

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Tobacco mosaic virus adsorption on self-assembled and Langmuir–Blodgett monolayers studied by TIRF and SFM

1998

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“…Nanostructures of thiol molecules serve as templates for attaching proteins. Selectivity of protein adsorption can be achieved by using the variation in protein affinity toward different SAMs (52)(53)(54)(55)(56)(57)(58).…”

Section: High-resolution Imaging and Fabricationmentioning

confidence: 99%

Positioning protein molecules on surfaces: A nanoengineering approach to supramolecular chemistry

Liu

Amro

2002

Proc. Natl. Acad. Sci. U.S.A.

183

158

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We discuss a nanoengineering approach for supramolecular chemistry and self assembly. The collective properties and biofunctionalities of molecular ensembles depend not only on individual molecular building blocks but also on organization at the molecular or nanoscopic level. Complementary to ''bottom-up'' approaches, which construct supramolecular ensembles by the design and synthesis of functionalized small molecular units or large molecular motifs, nanofabrication explores whether individual units, such as small molecular ligands, or large molecules, such as proteins, can be positioned with nanometer precision. The separation and local environment can be engineered to control subsequent intermolecular interactions. Feature sizes as small as 2 ؋ 4 nm 2 (32 alkanethiol molecules) are produced. Proteins may be aligned along a 10-nm-wide line or within two-dimensional islands of desired geometry. These high-resolution engineering and imaging studies provide new and molecular-level insight into supramolecular chemistry and self-assembly processes in bioscience that are otherwise unobtainable, e.g., the influence of size, separation, orientation, and local environment of reaction sites. This nanofabrication methodology also offers a new strategy in construction of two-and three-dimensional supramolecular structures for cell, virus, and bacterial adhesion, as well as biomaterial and biodevice engineering. S upramolecular chemistry has become an area of intense research (1-4), partly inspired by biological ensembles in nature, such as collagen and enzymes or protein assemblies in general. In nature, the collective properties and biofunctionalities of these ensembles depend not only on the individual molecular units but also (perhaps even more importantly) on the organization at the molecular or nanoscopic level (1, 2, 4, 5). Such organization dependence can be attributed to polyvalent interactions in biological systems (6). ''Bottom-up'' approaches have been taken to mimic nature and have resulted in creative synthesis of small molecular units (7,8) and large molecular motifs (9). These molecular building blocks contain the desired charge, polarization, or chemical functionalities that will affect intermolecular interactions such as van der Waals forces, hydrogen bonding, polar attractions, and͞or hydrophobic interactions (7-9). These interactions dictate the subsequent assembly into supramolecular structures (4, 9-11). Complementary to these synthetic approaches, we explore whether individual units such as small molecular ligands or large molecules such as proteins can be positioned with nanometer precision by using nanoengineering methodologies. The separation and local environment can be engineered to influence subsequent intermolecular interactions.Micrometer-sized patterns of biomolecules can be produced by using relatively well known microfabrication technologies. Without using templates, DNA micropatterns may be directly produced by using photolithography (12)(13)(14). Micropatterns of proteins have also been ...

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“…Since each of the two fluorescence contributions to the total fluorescence intensity can be separately determined in experiments and the concentration of the af488-HSA solution, c Sol , is known, the surface concentration of surface bound af488-HSA, Γ HSA , can, in principle, be calculated by finding the optical relationship between the two fluorescence components, I Ads and I Sol . The conversion from I Ads and I Sol to Γ HSA used in this study paralleled the quantification of protein adsorbed amount in total internal fluorescence microscopy [30,31] and will not be described in detail here (data not shown). The error in the measurement of the adsorbed HSA surface density was up to ±3.5% (estimated from the standard deviations of protein fluorescence intensity measured within OTS bands).…”

Section: Fluorescence Image Processing and Analysismentioning

confidence: 99%

Relating material surface heterogeneity to protein adsorption: the effect of annealing of micro-contact-printed OTS patterns

Hodgkinson¹,

Hlady²

2005

Journal of Adhesion Science and Technology

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We have investigated the influence of micrometer-and sub-micrometer-scale surface heterogeneities in patterned octadecyltrichlorosilane (OTS) films on human serum albumin (HSA) adsorption and its spatial distribution. 5-μm-wide OTS patterns were created on glass substrates by micro-contact printing and in some instances subsequent annealing was used to alter OTS molecule distribution within the patterns. Scanning force microscopy (SFM), advancing water contact angles and water vapor condensation figures were used to characterize the OTS films and to assess the nature of the heterogeneities within the various surface areas. High-resolution fluorescence microscopy was used to record images of fluorescently labeled albumin on OTS patterned films and fluorescence intensity was quantified and converted into the adsorbed amount. Adsorbed albumin was also characterized through SFM measurements. Combined SFM topography and lateral force microscopy (LFM) imaging revealed that micro-contact printing of OTS onto glass both replicated the stamp pattern and created small islands within the non-stamped regions between the patterns. The OTS coverage within stamped regions was not fully continuous but improved with subsequent annealing. Annealing also resulted in OTS island growth within the non-stamped regions and decreased average wettability on both the stamped and non-stamped areas. The extent of albumin adsorption was not proportional to OTS coverage, but correlated with the sub-μm distribution of OTS chains. We inferred that the surface distribution of ligands such as OTS on a sub-μm length scale determines the nature of albumin adsorption and its kinetics.

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Human Growth Hormone Adsorption Kinetics and Conformation on Self-Assembled Monolayers

Cited by 48 publications

References 26 publications

Tobacco mosaic virus adsorption on self-assembled and Langmuir–Blodgett monolayers studied by TIRF and SFM

Tobacco mosaic virus adsorption on self-assembled and Langmuir–Blodgett monolayers studied by TIRF and SFM

Positioning protein molecules on surfaces: A nanoengineering approach to supramolecular chemistry

Relating material surface heterogeneity to protein adsorption: the effect of annealing of micro-contact-printed OTS patterns

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