3 edition of The interaction of phospholipid surfaces with peptides and proteins found in the catalog.
The interaction of phospholipid surfaces with peptides and proteins
Josh Philip Kupferberg
Written in English
|LC Classifications||Microfilm 49795|
|The Physical Object|
|Pagination||xi, 222 l.|
|Number of Pages||222|
|LC Control Number||94895926|
The initiation and maintenance of an immune response to pathogens requires the interactions of cells and proteins that together are able to distinguish appropriate non-self targets from the myriadof self-proteins (Janeway and Bottomly, ). This discrimination between self and non-self is in part accomplished by three groups of proteins of the immune system that have direct and specific.
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This review aims to provide an introductory overview on protein and peptide interactions with phospholipid membranes and surfaces. Exemplifying such interactions for serum proteins and antimicrobial peptides (AMPs), key factors are addressed, including effects of membrane composition and of protein–peptide : M.
Malmsten. Download Citation | Protein and peptide interactions with phospholipid membranes and surfaces | This review aims to provide an introductory overview on protein and peptide interactions with.
Phospholipid interactions of the putative fusion peptide of hepatitis B surface antigen S protein we introduced mutations in HBV surface proteins to identify new motives necessary for viral. introduction outlining the importance of peptide-lipid and protein-lipid interactions to the functioning of biological systems.
It also outlines the aims and philosophy of this work. Section B relates the synthesis and purification of a series of 5 peptides used to model the lipid-protein interactions.
Cationic. peptides interactions with the phospholipid bilayer of membranes. Cationic peptides are attracted to the negatively charged prokaryotic membranes and kill microbial pathogens by causing disintegration of their membranes and subsequent collapse of electrochemical gradients [23, 30, 31].
Various models of membranolytic activities of Cited by: Rafalski M, Ortiz A, Rockwell A, Van Ginkel L, Lear J, DeGrado W, Wilschut J () Membrane fusion activity of the influenza virus hemagglutinin: Interaction of HA2 N-terminal peptides with phospholipid vesicles.
Biochemistry – PubMed CrossRef Google Scholar. The interaction of lipid environments with the type I’ β-turn peptide structure called CSF and its N-glucosylated form CSF(Glc), previously developed as a synthetic antigenic probe recognizing specific autoantibodies in a subpopulation of multiple sclerosis patients’ serum, was investigated by fluorescence spectroscopy and electrochemical experiments using large unilamellar vesicles.
The association of neuropeptide Y (NPY) with air−water interfaces and with phospholipid monolayers on water subphases and on physiological buffer has been investigated. Surface pressure (π) versus molecular area (A) relations of the peptide at water surfaces depend on the concentration of the spreading solutions.
Independent of that concentration, they show a transition from a low-density. Dynamic changes in the properties of adsorbed protein layers at material surfaces make it difficult to analyze a cell adhesion behavior.
Adhesion is affected by the ligand molecules in the adsorbed protein layers on the material’s surface. This study aimed to quantitatively analyze the initial cell adhesion onto a polymeric surface modified with immobilized cell adhesion molecules with a.
Peptides designed to model transmembrane helices, transmembrane helices of integral membrane proteins, and certain peptide ionophores such as alamethicin align more or less The interaction of phospholipid surfaces with peptides and proteins book across the bilayer; while the membrane-insertion sequences of SNARE proteins, and viral fusion peptides, integrate into the bilayer at an oblique angle.
In several cases, such interactions cause the insertion of the peptides to the membrane and their assembly within the lipid bilayer.
Here we present spectroscopic approaches utilizing NBD and rhodamine fluorescently labeled peptides to measure peptide–membrane interaction and peptide–peptide interaction within the membrane. Further observation reveals that the cell membrane is covered with abundant chiral biomolecules, such as amino acids, peptides, proteins, and glycans, which are either inserted into the phospholipid bilayers or modified on the head end of the phospholipid molecules.
This constructs an ideal chiral biointerface for the interaction with Aβ peptide. The Langmuir Blodgett apparatus provides a versatile system for studying the interfacial properties of peptides and peptide-membrane interactions under controlled conditions.
Using amphiphilic α-helical peptides to highlight studies undertaken, here we discuss the use of this system to provide information on the surface activity of peptides. The Langmuir Blodgett apparatus provides a versatile system for studying the interfacial properties of peptides and peptide-membrane interactions under controlled conditions.
langmuir blodgett, maximum surface pressure, monolayer, phospholipid, thermodynamic analysis, peptide, langmuir Protein & Peptide Letters () https. This is important in keeping a protein stable and biologically active, because it allow to the protein to decrease in surface are and reduce the undesirable interactions with water.
Besides from proteins, there are many other biological substances that rely on hydrophobic interactions for its survival and functions, like the phospholipid. Phospholipids. A phospholipid is a lipid that contains a phosphate group and is a major component of cell membranes.
A phospholipid consists of a hydrophilic (water-loving) head and hydrophobic (water-fearing) tail (see figure below). The phospholipid is essentially a triglyceride in which a fatty acid has been replaced by a phosphate group of some sort.
These proteins have a variety of functions, including transport and communication across the membrane.
Many integral membrane proteins are not in fixed position. They can move about, just as the phospholipid molecules do. Some membranes are crowded with proteins, but in others, the proteins are more sparsely distributed.
While the importance of protein adsorption to materials surfaces is widely recognized, little is understood at this time regarding how to design surfaces to control protein adsorption behavior. All-atom empirical force field molecular simulation methods have enormous potential to address this problem by providing an approach to directly investigate the adsorption behavior of peptides and.
To assess NPY association with phospholipid membrane surfaces, we started with dual-label experiments in which L-rhod B-DHPE (∼ mol% with respect to total lipid) was used to label the lipid monolayer while CF-hNPY (10 mol% with respect to total peptide) was used to visualize the peptide distribution at the surface.
Aggregation of amyloid beta (Aβ) peptides in neuronal membranes is a known promoter of Alzheimer’s disease. To gain insight into the molecular details of Aβ peptide aggregation and its effect on model neuronal membranes, we carried out molecular dynamics simulations of the Aβ(25–35) fragment of the amyloid precursor protein in phospholipid bilayers composed of either fully saturated or.
The interaction of antimicrobial peptides (AMPs) with biological membranes is in the focus of research since several years, and the most important features and modes of action of AMPs are described in this review.
Different model systems can be used to understand such interactions on a molecular lev. The hydrophobic effect is the observed tendency of nonpolar substances to aggregate in an aqueous solution and exclude water molecules.
The word hydrophobic literally means "water-fearing", and it describes the segregation of water and nonpolar substances, which maximizes hydrogen bonding between molecules of water and minimizes the area of contact between water and nonpolar molecules.
A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn 2+) in order to stabilize the ally coined to describe the finger-like appearance of a hypothesized structure from Xenopus laevis transcription factor IIIA, the zinc finger name has now come to encompass a wide variety of differing protein structures.
•Eight concentrations of each peptide (10 nM to 5 mM) were tested in the assay, allowing semi-quantitative measurement of the binding affinity of each peptide to its protein ligand Protein-DNA Interaction— •Protein microarrays have also been applied extensively and successfully to characterize protein-DNA interactions (PDIs).
We have now used reverse-phase high-performance liquid chromatography to determine the binding domains of peptides and, by extension, of proteins to a lipid surface. This approach consists of performing chemical modifications of specific amino acid side-chain functionalities after the interaction of the peptides with the reverse-phase high.
Interaction of transmembrane polypeptides with phospholipids on surface of lipid bilayer. Just on the surface of phospholipid bilayer, some amide residues do not participate in hydrogen bonding with anti-parallel strands of a transmembrane beta-barrel and remain free from beta-sheet formation (Figure 1).
In addition to dysregulation of phospholipid transporters, altered gene expression of multidrug-resistant proteins (ABC transporters), which can also function to outwardly transport phospholipids. The development of biomimetic surfaces for protein and peptide adsorptions is continuously expanding.
Their biological functions can be influenced by the properties of the underlying artificial environment but the detailed mechanism is still not clear. In the past 30 years, neutron reflectometry has been widely applied to characterise the molecular structure of proteins or multi-protein.
is involved in the interaction, while the rest of the protein is in contact with the mobile phase. The adsorption/desorption step takes place only once while the polypeptide is on the column.
After desorption, very little interaction takes place between the polypeptide and the reversed-phase surface and subsequent interactions have little. Phospholipids are a type of lipids that are a major component of cell membranes.
They can form lipid bilayers for their amphiphilic characteristic. The structure of a phospholipid molecule typically consists of two hydrophobic fatty acid "tails" and a hydrophilic "head" consisting of a phosphate group.
Peptides are smaller than proteins. Traditionally, peptides are defined as molecules that consist of between 2 and 50 amino acids, whereas proteins are made up of 50 or more amino acids.
In addition, peptides tend to be less well defined in structure than proteins, which can adopt complex conformations known as secondary, tertiary, and. In the present study, the interactions of different lecithin molecule head groups, namely PC, PE, and PI, with sucrose in cocoa butter medium are systematically examined based on our previous approach.
A similar technique was also used by Koeppen and Langel to explore adhesion forces of peptides on titanium dioxide surfaces. In the following. Cationic antimicrobial peptides are promising sources for novel therapeutic agents against multi-drug-resistant bacteria. HHC (KRWWKWWRR) is a simple but effective antimicrobial peptide with similar or superior activity compared with several conventional antibiotics.
In this biophysical study, un. To form polypeptides and proteins, amino acids are joined together by peptide bonds, in which the amino or NH 2 of one amino acid bonds to the carboxyl (acid) or COOH group of another amino acid.
A peptide is two or more amino acids joined together by peptide bonds; a polypeptide is a chain of many amino acids; and a protein contains one or.
CiteScore: ℹ CiteScore: CiteScore measures the average citations received per peer-reviewed document published in this title. CiteScore values are based on citation counts in a range of four years (e.g.
) to peer-reviewed documents (articles, reviews, conference papers, data papers and book chapters) published in the same four calendar years, divided by the number of. These polar interactions can be disrupted by adding salts or by changing the pH.
Many peripheral membrane proteins are bound to the surface of integral proteins on either the cytoplasmic or the extracellular side of the membrane. Secondary Structure of Membrane Proteins Proteins can span the membrane with alpha helices.
The archaeal protein. [link] Polar and charged amino acid residues (the remainder after peptide bond formation) are more likely to be found on the surface of soluble proteins where they can interact with water, and nonpolar (e.g., amino acid side chains) are more likely to be found in the interior where they are sequestered from water.
2 days ago This includes blocking viral receptors, inhibiting adsorption by antimicrobial binding peptides to viral proteins, interaction with co-receptors such as CXCR4, inhibition of cell fusion by interfering with the protein’s ATPase activity, inhibition of gene expression, inhibition of peptide elongation, and activation of immunomodulatory.
Role of peptides in prebiotic chemistry. Localizing RNA to membranes. In primitive cells, membranes may have played a catalytic role by co-localizing reactants on their surface. For example, the localization of RNAs to membranes could promote ribozyme assembly and facilitate ribozyme catalysis.
Generally speaking, the interaction of most peptides with eukaryotic membranes is inhibited by the lack of negatively charged lipids on the surface of such cells, by the rather low membrane potential (−15mV) across the plasma membrane of eukaryotic cells, and by the presence of cholesterol in the plasma membranes of such cells (compared to.
This thesis focuses on the study of interactions between protein and peptides and their potential applications in cell imaging and nanoparticle surface modification. Drawing inspiration from naturally occurring coiled-coil binding pairs, it proposes a novel covalent peptide tag and probe system.Introduction.
L antibiotics are gene-encoded antimicrobial peptides that are produced by and act on Gram-positive bacteria. They are structurally defined by the presence of intramolecular rings formed by the thioether amino acids lanthionine and methyllanthionine. 35 Lantibiotics are chemically and structurally very diverse; in addition to the characteristic thioether amino acids, numerous.
Membrane proteins play vital roles in every aspect of cellular activities. To study diverse membrane proteins, it is crucial to select the right surfactants to stabilize them for analysis.
Despite much effort, little progress has been made in elucidating their structure and function, largely because of a lack of suitable surfactants. Here we report the stabilization of a G protein-coupled.