Chemical Synthesis and Enzymic Processing of Precursor Forms of Cecropins A and B

Boman, Hans G.; Boman, I. A.; Andreu, David; Li, Zong-qu; Merrifield, R. B.; Schlenstedt, Gabriel; Zimmermann, Richard

doi:10.1016/s0021-9258(18)83628-6

Cited by 104 publications

(7 citation statements)

References 29 publications

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“…Antimicrobial peptides (AMPs), a class of organic endogenous protective peptides, play important roles in both biological innate immunity and acquired immunity ( Tornesello et al, 2020 ; Hancock et al, 2021 ; Li et al, 2021 ). Ever since Boman et al (1989) isolated cecropin from Hyalophora cecropia in 1975, more than a thousand species of AMPs derived from viruses, bacteria, plants, insects, mollusks, crustaceans, amphibians, fish, birds, and mammals have been confirmed and studied ( Waghu et al, 2016 ). Research has shown that AMPs have broad-spectrum antimicrobial effects, and their sterilization mechanism makes it difficult for pathogens to produce drug-resistant mutations ( Travkova et al, 2017 ; Savini et al, 2020 ).…”

Section: Introductionmentioning

confidence: 99%

Design, Synthesis, and Antitumor Activity Study of All-Hydrocarbon-Stapled B1-Leu Peptides

Liu

Cong

et al. 2022

Front. Chem.

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B1-Leu peptide is a structural optimization compound derived from the lysine- and phenylalanine-rich antimicrobial peptide Cathelicidin-BF. It has shown promising antibacterial and antitumor biological activity. However, linear peptides are not the best choice for novel drug development due to their poor pharmacokinetic properties. In this study, various all-hydrocarbon stapled B1-Leu derivatives were designed and synthesized. Their secondary structure, protease stability, and antitumor and hemolytic activities were also investigated to evaluate their clinical value for cancer therapy. Among them, B1-L-3 and B1-L-6 showed both damaging the tumor cell membrane stability and antitumor activity, showing that they are promising lead compounds for the development of novel cancer therapeutics.

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Section: Introductionmentioning

confidence: 99%

Design, Synthesis, and Antitumor Activity Study of All-Hydrocarbon-Stapled B1-Leu Peptides

Liu

Cong

et al. 2022

Front. Chem.

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“…We have used the following presecretory proteins as tools for gaining insights into the molecular details of how proteins are transported into the mammalian endoplasmic reticulum: silkworm preprocecropin A (Boman et al, Schlenstedt et al, 1989;Schlenstedt et al, 1990;Zimmermann et al, 1990), honeybee prepromelittin (Zimmermann and Mollay, 1986;Mfiller and Zimmermann, 1987;Miiller and Zimmermann, 1988a;M/iller and Zimmermann, 1988b;Zimmermann et al, 1988b), and frog prepropeptide GLa (Schlenstedt and Zimmermann, 1987). As an additional tool we have employed M13 procoat protein (Watts et aI., 1983;Wiech et al, 1987;Sagstetter and Zimmermann, 1988;Zimmermann et al, 1988aZimmermann et al, , 1990, the precursor of a bacterial plasma membrane protein.…”

Section: Resultsmentioning

confidence: 99%

Ribonucleoparticle-independent transport of proteins into mammalian microsomes

Zimmermann

Wiech

et al. 1990

J Bioenerg Biomembr

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There are at least two different mechanisms for the transport of secretory proteins into the mammalian endoplasmic reticulum. Both mechanisms depend on the presence of a signal peptide on the respective precursor protein and involve a signal peptide receptor on the cis-side and signal peptidase on the trans-side of the membrane. Furthermore, both mechanisms involve a membrane component with a cytoplasmically exposed sulfhydryl. The decisive feature of the precursor protein with respect to which of the two mechanisms is used is the chain length of the polypeptide. The critical size seems to be around 70 amino acid residues (including the signal peptide). The one mechanism is used by precursor proteins larger than about 70 amino acid residues and involves two cytosolic ribonucleoparticles and their receptors on the microsomal surface. The other one is used by small precursor proteins and relies on the mature part within the precursor molecule and a cytosolic ATPase.

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“…Furthermore, despite the lack of software available to analyze other post-translational modifications, the mature peptide can still be identified by homologous sequence alignment and prediction of cleavage sites ( Wang and Hu, 2017 ). In general, the N-terminus of a pro-AMP undergoes a two-step proteolytic cleavage by signal peptidase and dipeptidyl aminopeptidase ( Boman et al, 1989 ), while peptides with a Gly residue present at the C-terminus are subjected to an amide modification by a two-step sequential catalytic reaction with peptidylglycine α-amidating monooxygenase (PAM) ( Kim and Seong, 2001 ). Based on this bioinformatics analysis method, a total of 36 new, naturally occurring AMPs of butterfly origin were identified from the published genomic data used in the current study.…”

Section: Discussionmentioning

confidence: 99%

Identification and Characterization of Antimicrobial Peptides From Butterflies: An Integrated Bioinformatics and Experimental Study

Wang

Zhou

et al. 2021

Front. Microbiol.

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Butterflies represent one of the largest animal groups on Earth, yet antimicrobial peptides (AMPs) of this group are less studied in comparison with their moth counterparts. This study employed an integrated bioinformatics approach to survey natural AMPs from publicly available genomic datasets. Numerous AMPs, including cecropins, defensins, and moricins, were identified and subsequently used as templates for the design of a series of synthetic AMPs that mimicked the naturally occurring sequences. Despite differing biological effects among the various sequences, the synthetic AMPs exhibited potent antibacterial and antifungal activities in vitro and in vivo, without inducing hemolysis, which implied their therapeutic potential in infectious diseases. Electron and confocal fluorescence microscopies revealed that the AMPs induced distinct morphological and biophysical changes on microbial cell membranes and nuclei, suggesting that the antimicrobial effects were related to a mechanism of membrane penetration and nucleic acid binding by the peptides. In conclusion, this study not only offers insights into butterfly AMPs but also provides a practical strategy for high-throughput natural AMP discoveries that will have implications for future research in this area.

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Chemical Synthesis and Enzymic Processing of Precursor Forms of Cecropins A and B

Cited by 104 publications

References 29 publications

Design, Synthesis, and Antitumor Activity Study of All-Hydrocarbon-Stapled B1-Leu Peptides

Design, Synthesis, and Antitumor Activity Study of All-Hydrocarbon-Stapled B1-Leu Peptides

Ribonucleoparticle-independent transport of proteins into mammalian microsomes

Identification and Characterization of Antimicrobial Peptides From Butterflies: An Integrated Bioinformatics and Experimental Study

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