Open Access Pub
About Journal of Peptides
Journal of Peptides publishes peer-reviewed research on peptides as chemical and biological objects: how they are made, what shapes they hold, what they do, and what can be built from them.
The journal reads across peptide chemistry and synthesis, structure and function, bioactive and regulatory peptides, peptidomics and analysis, and the biological applications that follow from them.
What the journal covers
The whole molecule, not one use of it
Peptide work is one discipline read at several scales. A protecting-group decision changes what a synthesis can reach; a conformational constraint changes what a sequence can bind. The journal publishes across that span rather than at one point on it. The full statement of subject coverage, with the study types the journal considers, is on the Aims and Scope page.
- Chemistry and synthesisSolid-phase and solution-phase routes, protecting-group strategy, coupling and cyclization chemistry, noncanonical and modified residues, ligation, purification and characterization.
- Structure and functionConformational analysis, folding and constraint, spectroscopic, crystallographic and computational determination of structure, and the structure–activity relationships that follow from it.
- Bioactive and regulatory peptidesHormones and neuropeptides, antimicrobial and host-defense peptides, cell-penetrating and self-assembling sequences, receptor interaction and signaling.
- Analysis and applicationPeptidomics, mass spectrometry and analytical method development, peptide materials, and the biological, agricultural, food and pharmacological applications that build on them.
Why the field carries a journal of its own
A size regime with its own rules
Short enough to synthesize, long enough to be specific — the peptide scale is where chemistry can still build the molecule and biology already reads it.
Work at this scale answers to two sets of standards at once: the analytical standards of synthetic chemistry, and the controls expected of a biological measurement.
Peptides sit between small molecules and proteins, and they behave like neither. They are assembled residue by residue, so a sequence is a decision rather than a discovery, and a single substitution can be made and tested. At the same time they are long enough to fold, to present a surface, and to be recognized by a receptor or a membrane with the selectivity usually associated with much larger molecules.
That combination is why the questions in this field travel together. Stability, permeability and conformation are synthetic problems and biological ones in the same experiment, and a result reported without its synthesis and its characterization is difficult for anyone else to build on. A journal at this scale exists so that the chemistry and the biology of a peptide can be published in one place, in enough detail to be repeated.
Who the journal serves
Readers who need the method, not only the finding
The journal is written for people who will use a paper at the bench or at the keyboard, and it asks authors to report accordingly.
- Synthetic and medicinal chemistsResearchers designing routes, protecting-group strategies, cyclizations and modified residues, for whom the experimental section is the paper.
- Structural and computational scientistsGroups determining or predicting conformation, and relating it to binding, stability and activity.
- Biochemists and cell biologistsResearchers working on peptide signaling, processing, regulation and host defense, and on how sequences act in cells and tissues.
- Analytical and peptidomics groupsScientists developing identification, quantification and profiling methods, and applying them to complex samples.
- Applied and translational researchersTeams carrying peptide chemistry into agriculture, food science, materials and pharmacology, where the underlying molecule still has to be documented.
How the journal approaches scholarship
Editorial responsibility, stated plainly
Editorial decisions are independent of fees, services, membership and editorial or reviewing roles.
The full policy set is published on the Editorial Policies page.
Editors provide scholarly stewardship by overseeing peer review and upholding publication ethics. Editors recuse themselves from decisions on their own submissions, and those manuscripts are handled independently. The board is listed in full, with affiliations, on the Editorial Board page.
All submissions undergo initial editorial screening. Manuscripts that meet the journal's scope and minimum requirements proceed to independent peer review. Single-blind by default; double-blind review is available on request. Manuscripts that proceed to external peer review are normally evaluated by at least two independent subject-matter experts.
Editorial decisions are based on scope, scientific quality, methodological rigor, ethical compliance, reporting quality, and relevance to the journal. Reviewers are asked to assess experimental design, the adequacy of synthesis and characterization data, the interpretation of structural and biological results, and whether the work is reported in enough detail to be reproduced.
The journal is open access. Articles are published under the license stated on each article, and an article processing charge applies to accepted manuscripts; the current terms are on the Article Processing Charges page. Preparation and reporting requirements for each article type are set out in the Instructions for Authors.
Research continuity
Two records, opposite ends of one discipline
These illustrate the range the journal reads. They do not set its boundary: scope is stated on Aims and Scope, not inferred from the archive.
A review of macrocyclic design and a synthesis note on protecting a single side chain are the same subject at different magnifications — which is the case for publishing them in one journal.
Cyclic Peptides: Prominent Next Generation Targeted Therapies
Macrocyclization read as a design variable: phage display, genetic code expansion with noncanonical amino acids, and a range of cyclization chemistries, followed by the properties that constraining the backbone produces — affinity, metabolic stability and pharmacokinetic behavior between small molecules and biologics. The review also treats the same molecules as reagents, as selective probes and as imaging ligands.
Protection Side Chain of Lysine by Host-Affinity Molecules during Solid Phase Peptide Synthesis in Aqueous Phase
A protecting-group question answered by molecular recognition rather than by covalent chemistry: 18-crown-6 binds the lysine ε-amino group in its cavity through hydrogen bonding, so the side chain can be protected in aqueous phase instead of by reaction in organic solvent. The stated aims are to reduce organic-solvent use in solid-phase synthesis and to lower the cost of protecting lysine.
Submitting to Journal of Peptides
- Primary route: ManuscriptZone
- Alternative route: Simple manuscript submission form
- Assisted route: [email protected]
Authors must use only one submission route for the same manuscript.