What specific peptides or compounds make up gelatide formulations?
Executive summary
Gelatide formulations are not defined in the supplied reporting; available sources discuss peptide gelators broadly (short di‑ and tripeptides, protected peptide motifs, and collagen/gelatin‑derived peptide repeats) rather than a single commercial “gelatide” recipe [1] [2] [3]. Research papers describe classes of small peptide gelators identified by screening (e.g., nine dipeptides from a 2,025‑compound virtual library) and studies of tripeptide motifs and collagen‑derived repeated 30‑amino‑acid units used to make gelatin‑like materials [1] [2] [3].
1. What available reporting actually studies: small peptide gelators and gelatin repeats
Academic work cited here treats “peptide gelators” as a diverse research field, not a single product. Computational screening identified candidate dipeptides that self‑assemble into gels and nine dipeptides were synthesised and tested from a virtual library of 2,025 candidates [1] [4]. Separately, experimental soft‑matter work has focused on tripeptide motifs and their variants to map gelation behavior in organic media [2]. In a different strand, “gelatins” made by biotechnology are built from tandem repeats of longer collagen‑derived peptide units — studies report artificially designed gelatins comprising repeated 30‑amino‑acid peptide units derived from human α1 collagen [3].
2. What “peptides or compounds” recur in the literature
The common molecular themes across the sources are (a) very short peptides (di‑ and tri‑peptides) engineered or protected with hydrophobic/aromatic end groups to promote self‑assembly, and (b) longer collagen‑derived repeating peptide units used to make gelatin‑type materials. The computational screen explicitly concerns dipeptide structures that function as low‑molecular‑weight gelators [1]. The soft‑matter study examines a tripeptide motif and variants to understand assembly and processing in organic solvents [2]. The recombinant gelatin work uses tandemly repeated 30‑amino‑acid collagen‑related peptide units [3].
3. Where specifics are given — examples and scale
The computational study provides concrete numbers: a virtual library of 2,025 dipeptides was reduced by applicability‑domain filters to 699 candidates, and nine of those dipeptides were synthesized and tested as gelators [1]. The recombinant gelatin report describes engineered gelatins built from tandem repeats of 30‑amino‑acid units derived from human α1 collagen and produced in Bacillus brevis systems [3]. The soft‑matter paper characterizes assembly behavior for a tripeptide motif but the exact sequences and protecting groups are the article’s technical details [2].
4. What the sources do not say about “gelatide formulations”
None of the supplied sources define a commercial product called “gelatide” or list a standard formulation under that name; the term “gelatide” does not appear in the provided excerpts and therefore specific commercial ingredient lists or proprietary blends are not found in current reporting (not found in current reporting). The sources focus on scientific classes (dipeptide gelators, tripeptide motifs, collagen‑derived repeats) rather than a branded formulation [1] [2] [3].
5. Competing perspectives and implicit agendas to watch for
Academic papers emphasize fundamental mechanisms and broad “chemical space” for gelators — motivated by material science and biomedical applications — and favor publishing reproducible motifs and design rules [1] [2]. Industry pages about collagen peptides frame products as “compositions of different specific peptides optimized for physiological benefits,” an agenda to market ingredients for wellness or food uses that may elide sequence‑level detail [5]. Recombinant‑protein studies highlight production efficiency and sequence engineering for human‑like gelatins, with commercial scalability as a subtext [3].
6. Practical takeaways for readers seeking formulations
If you seek explicit ingredient lists for any product named “gelatide,” the supplied reporting does not provide them and you should consult manufacturer documentation or regulatory filings (not found in current reporting). If your interest is scientific — designing or selecting peptide gelators — the literature points to two practical classes to explore: low‑molecular‑weight di‑ and tri‑peptide gelators with hydrophobic/aromatic modifications, and longer collagen‑derived repeat peptides used to make gelatin‑like biomaterials [1] [2] [3].
Limitations: this analysis uses only the supplied search results; claims about formulations or proprietary recipes not mentioned in these sources are intentionally omitted [1] [2] [3].