Structural insights into Cn‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water
Open accessAbstract
Multifunctional and promiscuous antimicrobial peptides (AMPs) can be used as an efficient strategy to control pathogens. However, little is known about the structural properties of plant promiscuous AMPs without disulfide bonds. CD and NMR were used to elucidate the structure of the promiscuous peptide Cn‐AMP1, a disulfide‐free peptide isolated from green coconut water. Data here reported shows that peptide structure is transitory and could be different according to the micro‐environment. In this regard, Cn‐AMP1 showed a random coil in a water environment and an α‐helical structure in the presence of SDS‐d 25 micelles. Moreover, deuterium exchange experiments showed that Gly4, Arg5 and Met9 residues are less accessible to solvent, suggesting that flexibility and cationic charges seem to be essential for Cn‐AMP1 multiple activities.
AI snapshot
Written from the paper’s full text.
TL;DR
CD and NMR show that the disulfide-free plant peptide Cn-AMP1 is a random coil in water but adopts a largely α-helical structure in SDS-d25 micelles, with a helical segment from Ser-1 to Ala-6 (66.7%). H/D exchange identifies Gly-4, Arg-5, and Met-9 as less solvent-accessible, suggesting flexibility and a single cationic arginine contribute to its multifunctional activity.
Key findings
- In water, far-UV CD showed a random coil with a negative minimum at 190 nm; with SDS micelles, Cn-AMP1 acquired α-helical minima at 208 and 222 nm, with maximum α-helical content at 100 mM SDS. pH 3.97 gave the maximum conformation, while little variation was observed at pH 7.00.
- The NMR-derived structure in 100 mM SDS-d25 at pH 3.97 showed a helix between Ser-1 and Ala-6 (66.7% helical content) and no α-helix between Gln-7 and Met-9. The calculation used 118 distance restraints (43 intraresidual, 33 short-distance, 42 medium-distance; average 13.1 per residue), with RMSD 0.43 ± 0.16 Å for all atoms and 0.25 ± 0.19 Å for the α-helix; 95.1% of residues were in favored Ramachandran regions and 4.9% in allowed regions.
- H/D exchange showed that Gly-4, Arg-5, and Met-9 remained observable after 427 min and gave low-intensity correlations at 732 min, indicating lower solvent accessibility. Arg-5 was proposed as part of a possible membrane-interaction face.
- The structure indicated a hydrophobic rate of 25%, and glycine residues were discussed as providing flexibility important for antimicrobial function.
Methods
- Cn-AMP1 was synthesized by Fmoc solid-phase synthesis at 95% purity and confirmed by MALDI-ToF MS/MS. CD experiments used 50 µM peptide with 10, 20, 50, and 100 mM SDS in water, and at pH 3.97 and 7.00 with 100 mM SDS, collecting spectra from 190–260 nm at 25 °C.
- NMR data were acquired at 25 °C on a Bruker Avance III 500 spectrometer using 1.0 mM peptide with 100 mM SDS-d25 at pH 3.97; 2D 1H-1H TOCSY and NOESY experiments were recorded, and H/D exchange was monitored by TOCSY over 732 min.
- Structures were calculated with XPLOR-NIH by simulated annealing; 200 structures were generated and the 20 lowest-energy conformations were selected. Structural analysis used PROCHECK, PyMOL, and the Protein Interactions Calculator.
Limitations
- The paper does not state a formal limitations section; it notes that the all-atom RMSD (0.43 ± 0.16 Å) is below the usual optimal range but argues this is expected for a nine-residue peptide.
- Evident from the text: structural conclusions are based on water and SDS-d25 micelles, not native bacterial membranes, and no direct antimicrobial or cytotoxicity assays are reported in this structural study.
- Evident from the text: H/D exchange was performed only at pH 3.97 with 100 mM SDS-d25, and the small, flexible peptide may limit NOE-derived structural precision.
Model-written summary. Check it against the paper before relying on it.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
2 of 27 cited sources checked · 1 supported · 0 flagged · accuracy not yet measured
- Premisecitation
Other AMPs such as Pa-MAP1, PGLa, and LL37 show similar structural transitions.
“This idea was reinforced by the curiously parallel behavior observed here for other linear AMPs, including PGLa, a member of the magainin family [22], and LL37 [23]”
Quote in the paperNot a substantial claim2 of 3 sources checked- cites [21] source
The Discussion (page unavailable) describes a medium-dependent helix-to-coil transition for Pa-MAP, supporting that part of the claim. Our copy calls the peptide Pa-MAP, not Pa-MAP1, and does not establish comparable transitions for PGLa or LL37. (LLM, conf=0.86)
Experimental — accuracy not yet measured - cites [22] source
- cites [23] source
- Findingown data
H-bonds involving Arg-5-Ser-1, Arg-5-Val-2, and Ala-6-Val-2 stabilize the secondary structure of Cn-AMP1.
“H-bonds involving atoms between residues Arg-5-Ser-1; Arg5-Val-2 and Ala-6-Val-2 (Table S5) stabilize the secondary structure element and confirms the tendency of peptide to form an a-helical structure.”
Quote in the paperSubstantial claim - Findingown data
Only glycine residues of Cn-AMP1 are located in the lower energy stability region of the Ramachandran diagram.
“It is important to note that only glycine residues, which are known to provide great flexibility to peptide structure due to their low steric hindrance, are located in this region.”
Quote in the paperNot a substantial claim - Findingown data
Cn-AMP1 adopts a random coil conformation in aqueous solution.
“Cn-AMP1 showed a random coil in a water environment”
- Also stated in: § 3. Results and discussion · plain
“The far-UV CD spectrum of Cn-AMP1 in aqueous solution shows a typical spectrum of a peptide in a random coil conformation, with a negative minimum at 190 nm (Fig. 1A).”
- Also stated in: § 4. Conclusions · plain
“Cn-AMP1 showed a coil in a water environment”
Quote in the paperSubstantial claim - Also stated in: § 3. Results and discussion · plain
- Findingown data
In H/D exchange, after 427 min, correlations assigned to Hα of Gly-4, Gly-8, Arg-5, and Met-9 were observed.
“The correlations at d 3.80, d 3.86, d 4.24 and d 4.31 assigned to the H a of Gly-4, Gly-8, Arg-5 and Met-9, respectively, were observed after 427 min.”
Quote in the paperSubstantial claim
- Findingreasoning
Cn-AMP1 has no alpha-helical structure in the C-terminal portion between Gln-7 and Met-9.
“The molecule has also no a-helical structure in the C-terminal portion between Gln-7 and Met-9 residues.”
Quote in the paperNot a substantial claim - Findingown data
Most HN signals in the HN-Ha correlation region disappeared during H/D exchange, except those assigned to Gly-4, Arg-5, and Met-9.
“The NMR exchange experiment H/D showed that most of the H N signals of the H N -H a correlation region, responsible for the peptide interaction with the cell membrane, disappeared and only those correlations assigned to Gly-4, Arg-5 and Met-9 were still present.”
Quote in the paperSubstantial claim - Findingown data
At 732 min of H/D exchange, low intensity correlations remained for Gly-4, Arg-5, and Met-9.
“At the end of the experiment (732 min), low intensity correlations were observed in the chemical shift at d 3.78, d 4.12 and d 4.34, which were attributed to the H a of the Gly-4, Arg-5 and Met-9 residues, respectively (Fig. 4).”
Quote in the paperSubstantial claim - Findingown data
In the presence of SDS micelles, Cn-AMP1 adopts an alpha-helical structure characterized by minima at 208 and 222 nm.
“an a-helical structure in the presence of SDS-d 25 micelles”
- Also stated in: § 3. Results and discussion · plain
“When interacting with SDS micelles, the peptide acquired an a-helical fold, characterized by two minimums at 208 and 222 nm (Fig. 1B).”
- Also stated in: § 4. Conclusions · plain
“or an almost complete (66.7%) a-helical structure in the presence of SDS-d 25 micelles at pH 3.97”
Quote in the paperSubstantial claim - Also stated in: § 3. Results and discussion · plain
- Findingown data
Maximum alpha-helical content of Cn-AMP1 occurs at 100 mM SDS.
“The maximum a-helical content results occurred in the presence of 100 mM of SDS.”
Quote in the paperSubstantial claim - Interpretationown data
Flexibility and cationic charges presented by Gly-4, Arg-5, and Met-9 may be essential for Cn-AMP1 multiple activities.
“suggesting that flexibility and cationic charges seem to be essential for Cn-AMP1 multiple activities”
- Also stated in: § 4. Conclusions · hedged
“suggesting that flexibility and cationic charges presented by those residues may be essential for the development of Cn-AMP1 multiple activities”
Quote in the paperSubstantial claim - Also stated in: § 4. Conclusions · hedged
- Interpretationown data
Arg-5 is a possible interaction face of Cn-AMP1 with the cell membrane.
“The results of the exchange experiment and the presence of the positively charged residue (Arg-5) indicate that this is a possible interaction face with the cell membrane.”
Quote in the paperSubstantial claim- Rests on an assumption: SDS micelles are a valid model for the cell membrane, so the peptide's interaction with SDS micelles reflects its interaction with biological membranes.
- Interpretationown data
The Ramachandran diagram indicates a top structural quality for Cn-AMP1.
“Thus, the Ramachandran diagram indicates a top structural quality obtained for the peptide Cn-AMP1 (Fig. S4).”
Quote in the paperNot a substantial claim - Interpretationown data
CD and NMR analyses performed here provide the first structural elucidation of the disulfide-free multifunctional and promiscuous peptide from plant sources named Cn-AMP1.
“In summary, CD and NMR analyses performed here showed the first structural elucidation of the disulfide-free multifunctional and promiscuous peptide from plant sources named Cn-AMP1.”
Quote in the paperSubstantial claim - Interpretationown data
Gly-4, Arg-5, and Met-9 residues have low solvent accessibility due to interaction with the micelle.
“This suggests a low solvent accessibility of these residues due to the interaction with the micelle.”
Quote in the paperSubstantial claim - Interpretationcitation
The amphipathic profile of Cn-AMP1 seems important for interaction with the cell surface.
“This moment defines the amphipathic peptide profile, which seems to be important for interaction with the cell surface, as previously described, together with other multiple factors that included aggregation and charges [29].”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [29] source
- Interpretationcitation
Glycines in Cn-AMP1 could be important to antimicrobial function because they improve peptide flexibility.
“suggesting that glycines from Cn-AMP1 could be important to antimicrobial function since they improve peptide flexibility.”
Quote in the paperNot a substantial claim0 of 2 sources checked - Interpretationcitation
A single exposed Arg-5 in Cn-AMP1 is sufficient to start the antimicrobial activity process.
“Cn-AMP1 just shows a single Arg-5 exposed, which suggests that a single arginine is sufficient to start the antimicrobial activity process.”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [34] source
- Study design and conductown data
The molecular mass of Cn-AMP1 was confirmed and determined using MALDI-ToF MS/MS analysis.
“Cn-AMP1 was purified using reversed-phase HPLC, and molecular mass was confirmed and determined using MALDI-ToF MS/MS analysis (Autoflex, Bruker Daltonics, Billerica, MA).”
Quote in the paperNot a substantial claim - Interpretationown data
Cn-AMP1 has a possible region that could interact with negative surfaces, including bacterial membranes or nucleic acids.
“Fig. 4D shows a possible Cn-AMP1 region that could show clear interactivity with negative surfaces, including bacterial membranes or nucleic acids, which are common targets for antimicrobial peptides [28].”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [28] source
- Rests on an assumption: SDS micelles are a valid model for the cell membrane, so the peptide's interaction with SDS micelles reflects its interaction with biological membranes.
- Interpretationcitation
The data reported here corroborate the theoretical data presented for Cn-AMP1 by molecular modeling.
“Indeed, data reported here corroborate the theoretical data presented for Cn-AMP1 by using molecular modeling [9,11].”
Quote in the paperNot a substantial claim0 of 2 sources checked - Interpretationcitation
Conditions could directly affect multifunctional and promiscuous peptides.
“In summary, it seems that conditions could directly affect multifunctional and promiscuous peptides, as previously suggested by Franco [10]”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [10] source
- Interpretationown data
The structure of Cn-AMP1 is transitory and can differ according to the microenvironment.
“peptide structure is transitory and could be different according to the microenvironment”
- Also stated in: § 4. Conclusions · hedged
“Data reported here showed that peptide structure is transitory and could be different according to the micro-environment.”
Quote in the paperSubstantial claim - Also stated in: § 4. Conclusions · hedged
- Premisecitation
Cn-AMP1 is more active against four bacterial strains including Escherichia coli, Bacillus subtilis, Staphylococcus aureus and Pseudomonas aeruginosa.
“These three peptides showed deleterious activity against multiple Gram-positive and Gram-negative pathogenic bacteria, with Cn-AMP1 being more active against four bacterial strains including Escherichia coli, Bacillus subtilis, Staphylococcus aureus and Pseudomonas aeruginosa.”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [9] source
- Premisecitation
The antimicrobial activity of some peptides is largely governed by micro-environmental properties, especially at membrane levels.
“suggesting that their activity, especially at membrane levels, could be largely governed by micro-environmental properties, or in this case the constituent lipids [22].”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [22] source
- Premisecitation
Some antimicrobial peptide classes, such as human alpha-defensins and plant gamma-defensins, need arginines exposed on the peptide surface, and their removal or substitution reduced bacterial killing activity.
“It has been demonstrated that some antimicrobial peptide classes, such as human a-defensins [32] and plant c-defensins [33], need arginines exposed on the peptide surface and their removal or substitution reduced bacterial killing activity.”
Quote in the paperSubstantial claim0 of 2 sources checked - Premisecitation
Structural perturbation induced in selective peptides is much higher when compared to induction of non-selective peptides in the presence of lipids.
“These data indicate that structural perturbation induced in selective peptides is much higher when compared to induction of non-selective peptides in the presence of lipids.”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [24]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- May combine two claims. 11
- The quote only partly states this claim. 1
- Classified as probably not a substantial claim. 7
May combine two claims.
Findingown dataCn-AMP1 has a hydrophobic rate of 25% and an amphipathic profile defined by relative hydrophobic moment.
“calculations for this Cn-AMP1 structure indicated a hydrophobic rate of 25%, given the relative hydrophobic moment.”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataCn-AMP1 helical content varies little between pH 3.97 and pH 7.00 in 100 mM SDS, but pH 3.97 gives maximum conformation.
“Fig. 1C shows that little variation of Cn-AMP1 helical content was observed when both pHs were compared, but at pH 3.97 the peptide has a maximum conformation.”
Quote in the paperSubstantial claimMay combine two claims.
Findingown data95.1% of Cn-AMP1 residues are in alpha-helix favorable regions of the Ramachandran diagram, and 4.9% are in a region of lower energy stability.
“The peptide has a consistent distribution in the Ramachandran diagram, with 95.1% of the residue being located in a-helix favorable regions and only 4.9% of residues located in a region of lower energy stability.”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataThe NMR structure calculation used 118 distance restraints, with an average of 13.1 restrictions per residue, 43 intraresiduals, 33 short-distance and 42 medium-distance.
“After complete assignment, the volume of the correlations from the NOESY contour map were converted into distance, and 118 distance restraints were obtained, with an average of 13.1 restrictions per residue, 43 of these being intraresiduals, 33 short-distance and 42 medium-distance (Table S4).”
Quote in the paperNot a substantial claimThe quote only partly states this claim.
Findingown dataThe three-dimensional structure of Cn-AMP1 in 100 mM SDS-d25 at pH 3.97 contains an alpha-helix between Ser-1 and Ala-6, representing 66.7% helical content.
“The three-dimensional structure of Cn-AMP1 shows a helical structure between the Ser-1 and Ala-6 residues, which represents a helical content of 66.7%, a value previously predicted by in silico theoretical modeling [9].”
- Also stated in: § 4. Conclusions · plain
“Helical formation is showed in ribbon, between Ser-1 and Ala-6 residues”
Quote in the paperSubstantial claim- Also stated in: § 4. Conclusions · plain
May combine two claims.
Findingown dataThe RMSD for all atoms of the 20 lowest energy Cn-AMP1 structures is 0.43 ± 0.16 Å, and for the alpha-helix is 0.25 ± 0.19 Å.
“| RMSD (Å) all atoms | 0.43 ± 0.16 |”
- Also stated in: § 4. Conclusions · plain
“| RMSD (Å) a-helix | 0.25 ± 0.19 |”
Quote in the paperSubstantial claim- Also stated in: § 4. Conclusions · plain
Probably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductcitationCn-AMP1 was synthesized with 95% purity.
“Cn-AMP1 was purchased from the company Peptide 2.0 Incorporated (USA) which synthesized the peptide with 95% of purity after TFA removal by stepwise solid-phase synthesis using the N-9-fluorenylmethyloxycarbonyl (Fmoc) strategy [12].”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [12]
May combine two claims.
PremisecitationCn-AMP1 is a promiscuous peptide with activity against bacteria, fungi, cancer cells, and immunostimulatory activity.
“These features give the peptide Cn-AMP1 a promiscuous character, even not presenting disulfide bond connection [9,11].”
Quote in the paperSubstantial claim0 of 2 sources checkedMay combine two claims.
PremisecitationCn-AMP1 is a disulfide-free peptide isolated from green coconut water.
“Cn-AMP1, a disulfide-free peptide isolated from green coconut water”
- Also stated in: § 1. Introduction · plain
“Recently, three antimicrobial peptides were isolated from green coconut water (Cn-AMPs), in a series called Cn-AMP1 (SVAGRAQGM), Cn-AMP2 (TESYFVFSVGM) and Cn-AMP3 (YCSYTMEA) [9].”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [9] source
- Also stated in: § 1. Introduction · plain
Classified as probably not a substantial claim.
Study design and conductcitationThe quality of Cn-AMP1 structures was evaluated by analyzing the Ramachandran diagram from PROCHECK-NMR.
“Furthermore, the quality of Cn-AMP1 structures was evaluated by analyzing the Ramachandran diagram that is part of the PROCHECK-NMR software [18,25].”
Quote in the paperSubstantial claim0 of 2 sources checkedMay combine two claims.
InterpretationreasoningMet-9, which is not located in a helical region, lies immersed in the micelle, increasing the time required for exchange.
“In the case of the Met-9 residue, which is not located in a helical region, the lower susceptibility to exchange suggests that this residue must lie immersed in the micelle, increasing the time required for such an exchange.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
PremisecitationA glycine-rich antimicrobial peptide from guava seeds has numerous glycines that improve flexibility and seem involved in bactericidal activity.
“Moreover, a glycine-rich antimicrobial peptide isolated from guava seeds also showed numerous glycines that improve flexibility and seem to be closely involved in bactericidal activity [28]”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [28] source
Probably not a substantial claim: may not pass S3 (load-bearing), S4 (based).
Interpretationnone givenSelectivity against different cell types could be run by an electrostatic attraction between the peptide and cellular surface.
“Otherwise, selectivity against different cell types could be additionally run by an electrostatic attraction between the peptide and cellular surface.”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
PremisecitationThis perturbation is associated with peptide aggregation due to higher concentrations and peptide orientation caused by the presence of lipids.
“This perturbation is associated with peptide aggregation due to higher concentrations and peptide orientation caused by the presence of lipids.”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [24]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
PremisecitationSome peptides may adopt an alpha-helical structure able to disrupt DMPC and DMPG vesicles, or a beta-sheet structure only capable of permeabilizing DMPG vesicles.
“Some peptides may adopt, according to their primary structure and certain conditions, an a-helical structure able to disrupt DMPC and DMPG vesicles, in the case of non-selective peptides, or a b-sheet structure only capable of permeabilizing DMPG vesicles, in the case of selective peptides [24].”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [24]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
Probably not a substantial claim: may not pass S3 (load-bearing).
PremisecitationThe role of glycines in peptide flexibility was previously observed for other linear peptides.
“The role of glycines in peptide flexibility was previously observed for other linear peptides.”
Quote in the paperNot a substantial claim0 of 2 sources checked
The paper relies on this without support.
Little is known about the structural properties of plant promiscuous AMPs without disulfide bonds.
“However, little is known about structural properties in plant promiscuous AMPs without disulfide bonds.”
The paper relies on this without support.
SDS micelles are a valid model for the cell membrane, so the peptide's interaction with SDS micelles reflects its interaction with biological membranes.
“The NMR exchange experiment H/D showed that most of the H N signals of the H N -H a correlation region, responsible for the peptide interaction with the cell membrane, disappeared and only those correlations assigned to Gly-4, Arg-5 and Met-9 were still present.”
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
CnAMP1 strongly inhibits the growth of fungi and Gram-positive and Gram-negative bacteria.
“CnAMP1 (≈ 860 Da) strongly inhibits the growth of fungi and Gram-positive and Gram-negative bacteria [7].”
From The Coconut Water Antimicrobial Peptide CnAMP1 Is Taken up into Intestinal Cells but Does Not Alter P-Glycoprotein Expression and Activity (2020) · cites this paper as [7]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
Conflicting H2O:D2O ratios for the exchange experiment
MinorThe methods state that the lyophilized sample was dissolved in 60:40 H2O:D2O, whereas the caption for the resulting exchange spectra gives 40:60 H2O:D2O.
“The lyophilized material was then dissolved in H 2 O/D 2 O (60:40) at pH 3.97 and soon after a TOCSY spectrum was acquired as described previously.”
“(B) exchange TOCSY H/D, 40:60 (H 2 O:D 2 O), after 427 min; (C) exchange TOCSY H/D, 40:60 (H 2 O:D 2 O), after 732 min.”
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<i>Cn</i>‐AMP1: A new promiscuous peptide with potential for microbial infections treatment
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- 10.1016/j.peptides.2008.03.013 · DOI · Paper page
Cited by
Sorted by citations
Meneguetti, B. T., Machado, L. D. S., Oshiro, K. G. N., Nogueira, M. L., Carvalho, C. M. E., & Franco, O. L. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.02136 · Cited by 77 · see citing works
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Self-citationComposition, Properties and Reactions of Coconut Water
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- Authors
- Santana, M. J., de Oliveira, A. L., Queiroz Júnior, L. H. K., Mandal, S. M., Matos, C. O., de O. Dias, R., Franco, O. L., & Lião, L. M.
- Affiliations
- Universidade Federal de Goiás (BR)
- Indian Institute of Technology Kharagpur (IN)
- Corresponding author
- Lião, Luciano M.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2015-01-29
- Volume
- 589
- Issue
- 5
- Pages
- 639-644
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2150610432
- Semantic Scholar
- 7439d62e9c1c46357fe415c9f1dabb6d232c07cc
- Cited by
- 21
- References
- 37
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 2 · 2023: 1 · 2022: 2 · 2020: 2 · 2019: 2 · 2018: 6 · 2017: 1 · 2016: 2
- FWCI
- 2.21
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
- Conselho Nacional de Desenvolvimento Científico e Tecnológico
- Financiadora de Estudos e Projetos
- Fundação de Amparo à Pesquisa do Estado de Goiás
- Fundação de Apoio ao Desenvolvimento do Ensino, Ciência e Tecnologia do Estado de Mato Grosso do Sul
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Keywords
- antimicrobial peptides, green coconut water, plant antimicrobial peptides, peptide secondary structure, random coil, alpha-helix, micellar environment, hydrogen-deuterium exchange, solvent accessibility, cationic charge, peptide flexibility
- MeSH terms
- Amino Acid Sequence, Anti-Infective Agents, Circular Dichroism, Cocos, Disulfides, Magnetic Resonance Spectroscopy, Peptides
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Claims read by deepseek-v4.1-flash under definition version 3 (extract-v3) on 2026-10-10.
Classified by jev-1.13-20260917 (gold-guideline-v0.2) on 2026-10-10.
Cited sources are checked by gpt-6-sol.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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