Developing Polyamine-Based Peptide Amphiphiles with Tunable Morphology and Physicochemical Properties

Mehdi Bin Samad, Yashpal Singh Chhonker, Jacob I. Contreras, Alec McCarthy, Megan M. McClanahan, Daryl J Murry, Martin Conda Sheridan

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The ability to tune supramolecular properties such as size, morphology, or metabolic stability is of paramount importance in the field of supramolecular chemistry. Peptide amphiphiles (PAs) are a family of functional self-assembling biomaterials that have garnered widespread attention due to their broad applicability in medicine. PAs are generally comprised of an amino acid sequence connected to lipid tail(s) allowing them to self-assemble into supramolecular structures with diverse morphologies. Herein, this study describes the synthesis of a new class of polyamine-based “hybrid” PAs (PPAs) as novel self-assembling systems. The described molecules possess diverse polyamine head groups with the goal of tuning physicochemical properties. The findings indicate that small changes in the polyamine head groups result in altered PPA morphologies (nanofibers, micelles, nanoworms). The PPAs present a wide range of physicochemical characteristics, show superior resistance to aggregation, a diverse metabolic profile, and varied assembling kinetics. Most of the PPAs do not show toxicity in the human cells lines evaluated. The PPAs described herein hold promising potential as a safe and nontoxic option for drug delivery, targeting, and tissue engineering applications. (Figure presented.).

Original languageEnglish (US)
Article number1700096
JournalMacromolecular Bioscience
Volume17
Issue number8
DOIs
StatePublished - Aug 2017

Fingerprint

Amphiphiles
Polyamines
Peptides
Supramolecular chemistry
Nanofibers
Metabolome
Micelles
Biocompatible Materials
Drug Delivery Systems
Tissue Engineering
Drug delivery
Tissue engineering
Biomaterials
Lipids
Medicine
Toxicity
Tail
Amino acids
Amino Acid Sequence
Agglomeration

Keywords

  • nanostructures
  • peptide amphiphiles
  • polyamines
  • self-assembly

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

Cite this

Developing Polyamine-Based Peptide Amphiphiles with Tunable Morphology and Physicochemical Properties. / Samad, Mehdi Bin; Chhonker, Yashpal Singh; Contreras, Jacob I.; McCarthy, Alec; McClanahan, Megan M.; Murry, Daryl J; Conda Sheridan, Martin.

In: Macromolecular Bioscience, Vol. 17, No. 8, 1700096, 08.2017.

Research output: Contribution to journalArticle

Samad, Mehdi Bin ; Chhonker, Yashpal Singh ; Contreras, Jacob I. ; McCarthy, Alec ; McClanahan, Megan M. ; Murry, Daryl J ; Conda Sheridan, Martin. / Developing Polyamine-Based Peptide Amphiphiles with Tunable Morphology and Physicochemical Properties. In: Macromolecular Bioscience. 2017 ; Vol. 17, No. 8.
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