Effect of secondary structure on the potential of mean force for poly-l-lysine in the α-helix and β-sheet conformations

Grigsby, J.J.; Blanch, H.W.; Prausnitz, John M.

doi:10.1016/s0301-4622(02)00138-2

Cited by 47 publications

(34 citation statements)

References 21 publications

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“…For example, the coatings themselves are expensive and time‐consuming to prepare. Furthermore, PLL can demonstrate considerable variation in its secondary structure, which could correspondingly affect its activity, depending on the temperature, pH, and solvent polarity of the dissolving solution 1, 2. Moreover, laminin‐1 and fibronectin are instructive substrates that can activate neuronal receptors and signal transduction pathways,3 potentially interfering with the study of other neuroactive molecules.…”

Section: Introductionmentioning

confidence: 99%

Three‐dimensional nanofibrillar surfaces covalently modified with tenascin‐C‐derived peptides enhance neuronal growth in vitro

Ahmed

Liu

Mamiya

et al. 2005

J Biomedical Materials Res

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Current methods to promote growth of cultured neurons use two-dimensional (2D) glass or polystyrene surfaces coated with a charged molecule (e.g. poly-L-lysine (PLL)) or an isolated extracellular matrix (ECM) protein (e.g. laminin-1). However, these 2D surfaces represent a poor topological approximation of the three-dimensional (3D) architecture of the assembled ECM that regulates neuronal growth in vivo. Here we report on the development of a new 3D synthetic nanofibrillar surface for the culture of neurons. This nanofibrillar surface is composed of polyamide nanofibers whose organization mimics the porosity and geometry of the ECM. Neuronal adhesion and neurite outgrowth from cerebellar granule, cerebral cortical, hippocampal, motor, and dorsal root ganglion neurons were similar on nanofibers and PLL-coated glass coverslips; however, neurite generation was increased. Moreover, covalent modification of the nanofibers with neuroactive peptides derived from human tenascin-C significantly enhanced the ability of the nanofibers to facilitate neuronal attachment, neurite generation, and neurite extension in vitro. Hence the 3D nanofibrillar surface provides a physically and chemically stabile cell culture surface for neurons and, potentially, an exciting new opportunity for the development of peptide-modified matrices for use in strategies designed to encourage axonal regrowth following central nervous system injury.

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Section: Introductionmentioning

confidence: 99%

Three‐dimensional nanofibrillar surfaces covalently modified with tenascin‐C‐derived peptides enhance neuronal growth in vitro

Ahmed

Liu

Mamiya

et al. 2005

J Biomedical Materials Res

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“…The early kinetics (first 10 min) appear similar to the early adsorption of WLBU2 only (black dashes). However, the later kinetics are more consistent with the slower adsorption of S-WLBU2 (solid black), which is apparently driven by intermolecular interactions among peptides in the layer [30]. The increased resistance to elution by HClO 4 (Step 2) also suggests the existence of stabilizing intermolecular interactions between WLBU2 and S-WLBU2 in the PEO layer.…”

Section: Resultsmentioning

confidence: 89%

“…The initially fast adsorption followed by a slower increase observed in Step 1 of Figure 2b may be due to strong initial interactions between S-WLBU2 and the surface, followed by the promotion of intermolecular hydrogen bonding and hydrophobic interactions along the large surface area of the β -sheet to form dense aggregates. This results in continuing peptide adsorption at a slower rate [27, 30]. …”

Section: Resultsmentioning

confidence: 99%

Sequential and competitive adsorption of peptides at pendant PEO layers

Wu¹,

Ryder

McGuire

et al. 2015

Colloids and Surfaces B: Biointerfaces

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Earlier work provided direction for development of responsive drug delivery systems based on modulation of the structure, amphiphilicity, and surface density of bioactive peptides entrapped within pendant polyethylene oxide (PEO) brush layers. In this work, we describe the sequential and competitive adsorption behavior of such peptides at pendant PEO layers. Three cationic peptides were used for this purpose: the arginine-rich, amphiphilic peptide WLBU2, a peptide chemically identical to WLBU2 but of scrambled sequence (S-WLBU2), and the nonamphiphilic peptide poly-L-arginine (PLR). Optical waveguide lightmode spectroscopy (OWLS) was used to quantify the rate and extent of peptide adsorption and elution at surfaces coated with PEO. UV spectroscopy and time-of-flight secondary ion mass spectrometry (TOF-SIMS) were used to quantify the extent of peptide exchange during the course of sequential and competitive adsorption. Circular dichroism (CD) was used to evaluate conformational changes after adsorption of peptide mixtures at PEO-coated silica nanoparticles. Results indicated that amphiphilic peptides are able to displace adsorbed, non-amphiphilic peptides in PEO layers, while non-amphiphilic peptides were not able to displace more amphiphilic peptides. In addition, peptides of greater amphiphilicity dominated the adsorption at the PEO layer from mixtures with less amphiphilic or non-amphiphilic peptides.

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“…; for PLGA >50 000 a.u.) Literature data regarding the generation of random, α‐helix, and most of all β‐sheet structures from such samples report different conditions and therefore, the necessary first step was to establish pH, temperature and time ranges for the formation of a particular secondary structure in solution. According to our experiments, at pH 12, the water solution of PLL revealed a well resolved α‐helix conformation, whereas further heating to 52 °C for 15 minutes induced an α‐helix to β‐sheet transformation (Figure ).…”

Section: Resultsmentioning

confidence: 99%

Interactions of rationally designed small peptide dendrons functionalized with valine or sinapic acid with α‐helix and β‐sheet structures of poly‐l‐lysine and poly‐l‐glutamic acid

et al. 2020

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Uncontrolled protein oligomerization leading to deposition of fibrils is related to several diseases including neurodegeneration and diabetes. Involvement of natural compounds in regulation of this process has been documented. Therefore, the design and detailed study of bioinspired new molecular entities is one of the possible avenues to achieve better therapeutics. Here, we provide experimental data derived from the application of chiraloptic methods that rationally designed, bioinspired small branched peptides influenced the primary conformation of both poly-L-lysine (PLL) and poly-L-glutamic acid (PLGA) polypeptides in a structure-and concentrationdependent manner. In several cases, the circular dichroism (CD) spectra of polypeptide/dendron mixtures were considerably different from those corresponding to the individual polypeptides, in terms of significant reduction of intensity, discrete structure, and dislocation of characteristic bands. Data deconvolution suggested that compared to the individual homo-polypeptides, the resulting polypeptide/dendron complexes had a relative gain of distorted α-helix, and right-and left-hand twisted β-sheet forms, which may indicate a more diffuse structure. The electrostatic attraction and multiple hydrogen bonding between oppositely charged molecules, that is, between cationic-branched peptides and the β-sheet surface formed by anionic PLGA, might be the main cause of coaggregation that increased the variety and contribution of less ordered forms, and reduced the propensity for self-aggregation. K E Y W O R D S branched peptides, circular dichroism, fibrillation, sinapic acid, supramolecular interactions, valine

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Effect of secondary structure on the potential of mean force for poly-l-lysine in the α-helix and β-sheet conformations

Cited by 47 publications

References 21 publications

Three‐dimensional nanofibrillar surfaces covalently modified with tenascin‐C‐derived peptides enhance neuronal growth in vitro

Three‐dimensional nanofibrillar surfaces covalently modified with tenascin‐C‐derived peptides enhance neuronal growth in vitro

Sequential and competitive adsorption of peptides at pendant PEO layers

Interactions of rationally designed small peptide dendrons functionalized with valine or sinapic acid with α‐helix and β‐sheet structures of poly‐l‐lysine and poly‐l‐glutamic acid

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