scholarly journals Frontispiece: Peptide-Based Molecular Hydrogels as Supramolecular Protein Mimics

2017 ◽  
Vol 23 (5) ◽  
Author(s):  
Nishant Singh ◽  
Mohit Kumar ◽  
Juan F. Miravet ◽  
Rein V. Ulijn ◽  
Beatriu Escuder
Keyword(s):  
Protein Mimics

Scaffold optimization in discontinuous epitope containing protein mimics of gp120 using smart libraries

2013 ◽  
Vol 11 (16) ◽  
pp. 2676 ◽  
Author(s):  
Gwenn E. Mulder ◽  
H (Linda). C. Quarles van Ufford ◽  
Jeroen van Ameijde ◽  
Arwin J. Brouwer ◽  
John A. W. Kruijtzer ◽  
...  
Keyword(s):  
Discontinuous Epitope ◽  
Protein Mimics

scholarly journals An exhaustive survey of regular peptide conformations using a new metric for backbone handedness (h)

PeerJ ◽  
2017 ◽  
Vol 5 ◽  
pp. e3327 ◽  
Author(s):  
Ranjan V. Mannige
Keyword(s):  
Degrees Of Freedom ◽  
Intrinsically Disordered Proteins ◽  
Angular Displacement ◽  
Disordered Proteins ◽  
Dihedral Angles ◽  
Peptide Fragments ◽  
Ramachandran Plot ◽  
Peptide Backbone ◽  
Protein Mimics ◽  
Intrinsically Disordered

The Ramachandran plot is important to structural biology as it describes a peptide backbone in the context of its dominant degrees of freedom—the backbone dihedral angles φ and ψ (Ramachandran, Ramakrishnan & Sasisekharan, 1963). Since its introduction, the Ramachandran plot has been a crucial tool to characterize protein backbone features. However, the conformation or twist of a backbone as a function of φ and ψ has not been completely described for both cis and trans backbones. Additionally, little intuitive understanding is available about a peptide’s conformation simply from knowing the φ and ψ values of a peptide (e.g., is the regular peptide defined by φ = ψ =  − 100°  left-handed or right-handed?). This report provides a new metric for backbone handedness (h) based on interpreting a peptide backbone as a helix with axial displacement d and angular displacement θ, both of which are derived from a peptide backbone’s internal coordinates, especially dihedral angles φ, ψ and ω. In particular, h equals sin(θ)d∕|d|, with range [−1, 1] and negative (or positive) values indicating left(or right)-handedness. The metric h is used to characterize the handedness of every region of the Ramachandran plot for both cis (ω = 0°) and trans (ω = 180°) backbones, which provides the first exhaustive survey of twist handedness in Ramachandran (φ, ψ) space. These maps fill in the ‘dead space’ within the Ramachandran plot, which are regions that are not commonly accessed by structured proteins, but which may be accessible to intrinsically disordered proteins, short peptide fragments, and protein mimics such as peptoids. Finally, building on the work of (Zacharias & Knapp, 2013), this report presents a new plot based on d and θ that serves as a universal and intuitive alternative to the Ramachandran plot. The universality arises from the fact that the co-inhabitants of such a plot include every possible peptide backbone including cis and trans backbones. The intuitiveness arises from the fact that d and θ provide, at a glance, numerous aspects of the backbone including compactness, handedness, and planarity.

scholarly journals Optimal Hydrophobicity in Ring-Opening Metathesis Polymerization-Based Protein Mimics Required for siRNA Internalization

2016 ◽  
Vol 17 (6) ◽  
pp. 1969-1977 ◽  
Author(s):  
Brittany M. deRonde ◽  
Nicholas D. Posey ◽  
Ronja Otter ◽  
Leah M. Caffrey ◽  
Lisa M. Minter ◽  
...  
Keyword(s):  
Ring Opening ◽  
Ring Opening Metathesis Polymerization ◽  
Metathesis Polymerization ◽  
Protein Mimics

The design and synthesis of protein mimics

Peptides ◽  
1994 ◽  
pp. 310-312
Author(s):  
M. L. Smythe ◽  
M. von Itzstein
Keyword(s):  
Protein Mimics ◽  
Design And Synthesis

scholarly journals Applications of Dendrimers in Drug Delivery Agents, Diagnosis, Therapy, and Detection

2014 ◽  
Vol 2014 ◽  
pp. 1-19 ◽  
Author(s):  
B. Noriega-Luna ◽  
Luis A. Godínez ◽  
Francisco J. Rodríguez ◽  
A. Rodríguez ◽  
G. Zaldívar-Lelo de Larrea ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Three Dimensional ◽  
Modified Electrodes ◽  
Biologically Active ◽  
Protein Mimics ◽  
Chemically Modified ◽  
Biological Compatibility ◽  
Variable Chemical ◽  
Diagnostic Applications ◽  
Diagnosis Therapy

In recent years, the application of dendrimers in biomedicine attracted much attention from scientists. Dendrimers are interesting for biomedical applications because of their characteristics, including: a hyperbranching, well-defined globular structures, excellent structural uniformity, multivalency, variable chemical composition, and high biological compatibility. In particular, the three-dimensional architecture of dendrimers can incorporate a variety of biologically active agents to form biologically active conjugates. This review of dendrimers focuses on their use as protein mimics, drug delivery agents, anticancer and antiviral therapeutics, and in biomedical diagnostic applications such as chemically modified electrodes.

Shape-specific nanostructured protein mimics from de novo designed chimeric peptides

2018 ◽  
Vol 6 (2) ◽  
pp. 272-279 ◽  
Author(s):  
Linhai Jiang ◽  
Su Yang ◽  
Reidar Lund ◽  
He Dong
Keyword(s):  
Self Assembly ◽  
De Novo ◽  
Protein Mimics ◽  
Trigonal Bipyramidal ◽  
Chimeric Peptides

We experimentally and theoretically demonstrated the formation of well-defined trigonal-bipyramidal protein-mimics through self-assembly of “simple” de novo designed chimeric peptides.

scholarly journals De novo design of protein mimics of B-DNA

2016 ◽  
Vol 12 (1) ◽  
pp. 169-177 ◽  
Author(s):  
Deniz Yüksel ◽  
Piero R. Bianco ◽  
Krishna Kumar
Keyword(s):  
De Novo ◽  
De Novo Design ◽  
Protein Mimics

Structural mimicry of DNA is utilized in nature as a strategy to evade molecular defences mounted by host organisms.

scholarly journals BrucellaTIR Domain-containing Protein Mimics Properties of the Toll-like Receptor Adaptor Protein TIRAP

2009 ◽  
Vol 284 (15) ◽  
pp. 9892-9898 ◽  
Author(s):  
Girish K. Radhakrishnan ◽  
Qiqi Yu ◽  
Jerome S. Harms ◽  
Gary A. Splitter
Keyword(s):  
Adaptor Protein ◽  
Toll Like Receptor ◽  
Protein Mimics
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