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Special Issue "Recent Advances in Self-Assembled Peptides"

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Chemical Biology".

Deadline for manuscript submissions: 1 February 2019

Special Issue Editor

Guest Editor
Assoc. Prof. Dr. He Dong

Department of Chemistry and Biochemistry, The University of Texas at Arlington, Arlington, Texas 76019-0065, USA
Website | E-Mail
Interests: De novo peptide design and self-assembly; bioorganic chemistry; supramolecular chemistry; antimicrobial peptides; cell penetrating peptides; peptide–polymer conjugates; cancer nanotechnology; antimicrobial nanomaterials; drug delivery; gene delivery; self-assembling hydrogel

Special Issue Information

Dear Colleagues,

The last two decades have witnessed great achievements in the design and self-assembly of peptides to generate functional materials. Peptides, as the molecular building blocks, can be either de novo designed or engineered, based on naturally derived sequences that self-assemble into highly ordered nanostructures and nanostructured networks. From a fundamental viewpoint, the self-assembly strategy, in combination with new peptide design principles and chemistry has provided powerful tools to fabricate a wide range of thermodynamically stable and kinetically trapped nanostructures, as well as dynamic and smart nanostructures and materials in response to specific triggers. Comprehensive structural characterization of these hierarchical structures and fundamental analysis and understanding of their thermodynamics and kinetics are crucial to develop self-assembled, well-regulatedpeptides. From the viewpoint of practical applications, the main focus is to develop optimal functionality of self-assembled peptides. Pre-functionalization of the molecular building blocks and post-modification of the self-assembly are both effective methods to endow functions on self-assembled peptides and both are being extensively explored with regard to a variety of nanotechnological and biotechnological applications.

The main aim of this Special Issue is to create an open forum where researchers can share their new methods, results, perspectives and insights, and work together to address emerging issues of both fundamental and practical significance in peptide self-assembly. Contributions to this issue, both in the form of original research or review articles, may cover all aspects of peptide self-assembly and multidisplinnary studies offering new principles, methodologies/strategies and insights are particularly welcome.

Assoc. Prof. Dr. He Dong
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.


  • De novo peptide design and self-assembly
  • Computational approaches in the design of self-assembling peptides
  • Microscopic/spectroscopic tools for the study of self-assembling peptide structures
  • Functional peptide nanomaterials
  • Stimuli-responsive peptide self-assembly
  • Peptide-based hydrogels
  • Hybrid peptide-based materials
  • Biointerface and microdevices based on self-assembled peptides
  • Technological and biomedical applications of self-assembled peptides

Published Papers (1 paper)

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Open AccessArticle Shape Effects of Peptide Amphiphile Micelles for Targeting Monocytes
Molecules 2018, 23(11), 2786; https://doi.org/10.3390/molecules23112786
Received: 24 September 2018 / Revised: 23 October 2018 / Accepted: 25 October 2018 / Published: 27 October 2018
PDF Full-text (4377 KB) | HTML Full-text | XML Full-text | Supplementary Files
Peptide amphiphile micelles (PAMs) are a nanoparticle platform that have gained popularity for their targeting versatility in a wide range of disease models. An important aspect of micelle design is considering the type of hydrophobic moiety used to synthesize the PAM, which can
[...] Read more.
Peptide amphiphile micelles (PAMs) are a nanoparticle platform that have gained popularity for their targeting versatility in a wide range of disease models. An important aspect of micelle design is considering the type of hydrophobic moiety used to synthesize the PAM, which can act as a contributing factor regarding their morphology and targeting capabilities. To delineate and compare the characteristics of spherical and cylindrical micelles, we incorporated the monocyte-targeting chemokine, monocyte chemoattractant protein-1 (MCP-1), into our micelles (MCP-1 PAMs). We report that both shapes of nanoparticles were biocompatible with monocytes and enhanced the secondary structure of the MCP-1 peptide, thereby improving the ability of the micelles to mimic the native MCP-1 protein structure. As a result, both shapes of MCP-1 PAMs effectively targeted monocytes in an in vitro binding assay with murine monocytes. Interestingly, cylindrical PAMs showed a greater ability to attract monocytes compared to spherical PAMs in a chemotaxis assay. However, the surface area, the multivalent display of peptides, and the zeta potential of PAMs may also influence their biomimetic properties. Herein, we introduce variations in the methods of PAM synthesis and discuss the differences in PAM characteristics that can impact the recruitment of monocytes, a process associated with disease and cancer progression. Full article
(This article belongs to the Special Issue Recent Advances in Self-Assembled Peptides)

Graphical abstract

Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Title: Engineering Peptide-based Polyelectrolyte Complexes with Increased Hydrophobicity
Authors: Sara Tabandeh and Lorraine Leon

Title: Inner-Directed Transmembrane Self-Assembly of Cyclic Peptides: It´s What´s Inside that Counts
Author: Rebeca García Fandiño

Author: Shi‐Zhong Luo
Abstract: Fused in sarcoma (FUS) is a DNA / RNA binding protein, which is involved in RNA metabolism and DNA repair. Numerous reports have demonstrated that FUS is associated with a variety of neurodegenerative diseases by pathological and genetic analysis, including amyotrophic lateral sclerosis(ALS), frontotemporal lobar degeneration (FTLD) and polyglutamine diseases. Traditionally it was considered that the fabric aggregation of FUS caused those diseases, especially via its prion-like domains(PrLDs), rich in glutamine and asparagine resides. Lately, a non-fabric self-assembling phenomenon, liquid-liquid phase separation (LLPS) was observed in FUS and the studies of its functions, mechanism and mutual transformation with pathogenic amyloid were emerging. This review summarizes recent studies on FUS self-assembling, including both aggregation and LLPS, and their relationship with the pathology of ALS, FTLD and other neurodegenerative diseases.


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