The DOI matches its Crossref record.
‘100 years of peptide synthesis’: ligation methods for peptide and protein synthesis with applications to β‐peptide assemblies*
Abstract
Abstract: A brief survey of the history of peptide chemistry from Theodore Curtius to Emil Fischer to Bruce Merrifield is first presented. The discovery and development of peptide ligation, i.e. of actual chemical synthesis of proteins are described. In the main chapter, ‘Synthesis of Proteins by Chemical Ligation’ a detailed discussion of the principles, reactivities and mechanisms involved in the various coupling strategies now applied (ligation, chemical ligation, native chemical ligation) is given. These include coupling sites with cysteine and methionine (as well as the seleno analogs), histidine, glycine and pseudo‐prolines, ‘unrestricted’ amino‐acid residues (using the Staudinger reaction), as well as solid‐phase segment coupling by thioligation of unprotected peptides. In another section, ‘Synthesis of β‐peptides by Thioligation’, couplings involving β2‐ and β3‐peptides are described (with experimental details).
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
No references could be resolved yet.
Research works printed but not linked: 119
- 10.1002/cber.190103402249 · DOI · Paper page
- 10.1002/prac.18820260112 · DOI
- 10.1002/prac.19040700103 · doi:10.1002/prac.19040700103
- 10.1002/cber.190503801103 · doi:10.1002/cber.190503801103
- 10.1042/bj0291602 · DOI
- Sifferd R.H., 1935, A new synthesis of carnosine, with some observations on the splitting of the benzyl group from carbobenzoxy derivatives and from benzylthioethers, J. Biol. Chem., 108, 753, 10.1016/S0021-9258(18)75265-4 · DOI · Paper page
- 10.1021/ja01641a004 · DOI · Paper page
- 10.1021/ja01573a050 · doi:10.1021/ja01573a050
- 10.1021/ja01574a029 · DOI · Paper page
- 10.1038/199172b0 · DOI
- 10.1021/ja01609a099 · DOI · Paper page
- Khorana H.G., 1955, The use of dicyclohexylcarbodiimide in the synthesis of peptides, Chem. Ind. (London), 33, 1087
- 10.1016/0040-4020(67)80037-1 · DOI
- 10.1021/ja00897a025 · DOI · Paper page
- 10.1021/ja00359a014 · DOI · Paper page
- 10.1021/ja00722a043 · DOI · Paper page
- Aguilar M.‐I., 2004, HPLC of Peptides and Proteins: Methods and Protocols
- 10.1385/1592590454 · DOI
- Gutte B., 1971, The synthesis of ribonuclease A, J. Biol. Chem., 246, 1922, 10.1016/S0021-9258(18)62396-8 · DOI · Paper page
- 10.1073/pnas.86.19.7397 · DOI
- Chun R., 1990, Chemical synthesis of biologically active tat trans‐activating protein of human immunodeficiency virus type I, J. Virol., 64, 3074, 10.1128/jvi.64.6.3074-3077.1990 · doi:10.1128/jvi.64.6.3074-3077.1990
- 10.1073/pnas.95.23.13549 · doi:10.1073/pnas.95.23.13549
- 10.1073/pnas.91.9.4044 · DOI
- 10.1016/S1359-0278(98)00066-2 · DOI
- 10.1002/jlac.19535830110 · DOI · Paper page
- 10.1016/0040-4039(81)80049-4 · doi:10.1016/0040-4039(81)80049-4
- 10.1016/0040-4039(81)80050-0 · doi:10.1016/0040-4039(81)80050-0
- 10.1021/jo00360a033 · doi:10.1021/jo00360a033
- 10.1021/jo00367a013 · doi:10.1021/jo00367a013
- 10.1021/jo00273a008 · doi:10.1021/jo00273a008
- 10.1126/science.1566069 · DOI · Paper page
- 10.1126/science.2686029 · DOI · Paper page
- 10.1126/science.7973629 · DOI · Paper page
- 10.1021/ja962656r · DOI · Paper page
- 10.1073/pnas.96.18.10068 · DOI · Paper page
- 10.1021/ja960812o · doi:10.1021/ja960812o
- 10.1016/0040-4039(95)00037-D · doi:10.1016/0040-4039(95)00037-d
- 10.1021/ja00116a005 · DOI
- Tam J.P., 1995, Peptide synthesis using unprotected peptides through orthogonal coupling methods, Proc. Natl Acad. Sci. USA, 92, 12485, 10.1073/pnas.92.26.12485 · DOI · Paper page
- 10.1021/ja983859d · DOI
- 10.1021/ja9621105 · DOI · Paper page
- 10.1021/ja992668n · doi:10.1021/ja992668n
- 10.1039/c29710000636 · DOI · Paper page
- 10.1021/jo981990y · DOI · Paper page
- 10.1021/ol0060836 · doi:10.1021/ol0060836
- 10.1002/1521-3773(20010917)40:18<3395::AID-ANIE3395>3.0.CO;2-G · doi:10.1002/1521-3773(20010917)40:18<3395::aid-anie3395>3.0.co;2-g
- 10.1146/annurev.biochem.72.121801.161900 · DOI · Paper page
- 10.1073/pnas.0305693101 · doi:10.1073/pnas.0305693101
- 10.1126/science.282.5397.2220 · DOI · Paper page
- 10.1021/ja0491836 · DOI · Paper page
- 10.1021/ja00076a010 · doi:10.1021/ja00076a010
- 10.1021/ja037988s · DOI
- 10.1146/annurev.biochem.69.1.923 · DOI · Paper page
- 10.1002/(SICI)1097-0282(19981015)46:5<319::AID-BIP3>3.0.CO;2-S · DOI
- Heinrikson R.L., 1971, The selective S‐methylation of sulfhydryl groups in proteins and peptides with methyl‐p‐nitrobenzenesulfonate, J. Biol. Chem., 246, 4090, 10.1016/S0021-9258(18)62144-1 · doi:10.1016/s0021-9258(18)62144-1
- 10.1002/1522-2675(20010516)84:5<1197::AID-HLCA1197>3.0.CO;2-# · doi:10.1002/1522-2675(20010516)84:5<1197::aid-hlca1197>3.0.co;2-#
- 10.1039/b208288h · DOI
- 10.1021/ol015712o · doi:10.1021/ol015712o
- 10.1002/1439-7633(20020802)3:8<709::AID-CBIC709>3.0.CO;2-8 · doi:10.1002/1439-7633(20020802)3:8<709::aid-cbic709>3.0.co;2-8
- 10.1002/anie.200250830 · DOI
- 10.1021/ja00194a064 · doi:10.1021/ja00194a064
- Luthra N.P., 1981, Demonstration of the feasibility of observing nuclear magnetic resonance signals of 77Se covalently attached to proteins, J. Biol. Chem., 257, 1142, 10.1016/S0021-9258(19)68164-0 · doi:10.1016/s0021-9258(19)68164-0
- 10.1016/S0040-4039(96)02260-5 · DOI · Paper page
- 10.1021/ja960398s · DOI · Paper page
- 10.1021/ol991184t · doi:10.1021/ol991184t
- 10.1021/ol0157813 · doi:10.1021/ol0157813
- 10.1016/S0960-894X(02)00319-0 · doi:10.1016/s0960-894x(02)00319-0
- 10.1016/j.bmc.2004.02.039 · doi:10.1016/j.bmc.2004.02.039
- 10.1016/S0040-4039(03)01463-1 · doi:10.1016/s0040-4039(03)01463-1
- 10.1021/ja00089a001 · DOI · Paper page
- 10.1073/pnas.91.14.6584 · DOI · Paper page
- 10.1021/ja991153t · DOI · Paper page
- 10.1002/(SICI)1097-0282(1999)51:5<311::AID-BIP2>3.0.CO;2-A · DOI
- 10.1021/ja954278g · DOI
- 10.1016/S0040-4020(01)96019-3 · doi:10.1016/s0040-4020(01)96019-3
- 10.1002/hlca.19920750326 · doi:10.1002/hlca.19920750326
- 10.1002/anie.199627081 · doi:10.1002/anie.199627081
- 10.1021/ja000128g · DOI
- 10.1021/jm000920s · doi:10.1021/jm000920s
- 10.1021/ja00119a001 · DOI · Paper page
- 10.1021/ja00080a004 · doi:10.1021/ja00080a004
- 10.1016/j.tetlet.2003.10.126 · doi:10.1016/j.tetlet.2003.10.126
- 10.1021/ol0060174 · DOI · Paper page
- 10.1021/ol006739v · DOI · Paper page
- 10.1021/jo025631l · doi:10.1021/jo025631l
- 10.1021/ja029752e · doi:10.1021/ja029752e
- 10.1126/science.287.5460.2007 · DOI · Paper page
- 10.1021/ol006054v · DOI · Paper page
- 10.1002/hlca.19190020164 · DOI · Paper page
- 10.1016/S0040-4020(01)92229-X · doi:10.1016/s0040-4020(01)92229-x
- 10.1002/anie.200401744 · DOI · Paper page
- 10.1021/ja9836287 · doi:10.1021/ja9836287
- 10.1021/jo000346s · doi:10.1021/jo000346s
- 10.1002/hlca.19960790402 · DOI · Paper page
- 10.1002/cbdv.200490087 · DOI · Paper page
- 10.1002/(SICI)1521-3773(19990601)38:11<1595::AID-ANIE1595>3.0.CO;2-0 · doi:10.1002/(sici)1521-3773(19990601)38:11<1595::aid-anie1595>3.0.co;2-0
- 10.1002/hlca.19960790802 · DOI
- 10.1002/hlca.19970800703 · DOI · Paper page
- 10.1002/1522-2675(200209)85:9<2577::AID-HLCA2577>3.0.CO;2-D · doi:10.1002/1522-2675(200209)85:9<2577::aid-hlca2577>3.0.co;2-d
- 10.1002/anie.200250290 · doi:10.1002/anie.200250290
- 10.1021/jm010816q · doi:10.1021/jm010816q
- 10.1002/(SICI)1522-2675(19991006)82:10<1774::AID-HLCA1774>3.0.CO;2-O · DOI · Paper page
- 10.1002/cbdv.200490136 · doi:10.1002/cbdv.200490136
- 10.1002/cbdv.200490102 · doi:10.1002/cbdv.200490102
- 10.2533/chimia.1998.734 · DOI
- 10.1002/1439-7633(20020503)3:5<424::AID-CBIC424>3.0.CO;2-0 · doi:10.1002/1439-7633(20020503)3:5<424::aid-cbic424>3.0.co;2-0
- 10.1002/cbic.200300827 · doi:10.1002/cbic.200300827
- Guichard G., 1997, Solid‐phase synthesis of β‐oligopeptides, Chimia, 51, 315, 10.2533/chimia.1997.315 · doi:10.2533/chimia.1997.315
- 10.1002/hlca.19980810202 · doi:10.1002/hlca.19980810202
- 10.1002/hlca.200390149 · doi:10.1002/hlca.200390149
- 10.1002/bip.20088 · DOI · Paper page
- 10.1002/1522-2675(20001220)83:12<3139::AID-HLCA3139>3.0.CO;2-W · doi:10.1002/1522-2675(20001220)83:12<3139::aid-hlca3139>3.0.co;2-w
- 10.1002/hlca.200390133 · DOI
- 10.1002/1522-2675(200206)85:6<1812::AID-HLCA1812>3.0.CO;2-E · doi:10.1002/1522-2675(200206)85:6<1812::aid-hlca1812>3.0.co;2-e
- 10.1016/j.tet.2004.06.043 · DOI
- 10.1002/hlca.200390337 · doi:10.1002/hlca.200390337
- 10.1002/hlca.200490142 · DOI
- 10.1021/ja026114n · DOI
- 10.1016/0003-2697(76)90034-8 · doi:10.1016/0003-2697(76)90034-8
Cited by
Adding New Chemistries to the Genetic Code
Liu, C. C., & Schultz, P. G. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.105824 · Cited by 1,725
Vasudev, P. G., Chatterjee, S., Shamala, N., & Balaram, P. (2011) · Chemical Reviews · doi:10.1021/cr100100x · Cited by 329
Microreactor Synthesis of β‐Peptides
Flögel, O., Codée, J. D. C., Seebach, D., & Seeberger, P. H. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200602167 · Cited by 108
Ynamide Coupling Reagents: Origin and Advances
Hu, L., & Zhao, J. (2024) · Accounts of Chemical Research · doi:10.1021/acs.accounts.3c00743 · Cited by 89
Ynamide‐Mediated Peptide Bond Formation: Mechanistic Study and Synthetic Applications
Xu, S., Jiang, D., Peng, Z., Hu, L., Liu, T., Zhao, L., & Zhao, J. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202212247 · Cited by 46
Metadata
- Authors
- Kimmerlin, T., & Seebach, D.
- Venue
- The Journal of Peptide Research
- Publisher
- Wiley
- Published
- 2005-02
- Volume
- 65
- Issue
- 2
- Pages
- 229-260
- ISSN
- 1397-002X (ISSN-L)
- OpenAlex
- W1608917806
- Cited by
- 190
- References
- 0
- FWCI
- 4.61
- Type
- journal article
- Language
- en
- Open access
- closed
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.
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.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: ‘100 years of peptide synthesis’: ligation methods for peptide and protein synthesis with applications to β‐peptide assemblies*. https://app.cochat.ai/papers/10.1111/j.1399-3011.2005.00214.x
- The paper
- Kimmerlin, T., & Seebach, D. (2005). ‘100 years of peptide synthesis’: ligation methods for peptide and protein synthesis with applications to β‐peptide assemblies*. The Journal of Peptide Research. https://doi.org/10.1111/j.1399-3011.2005.00214.x
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.