Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Structure and Nomenclature of Thiols and Sulfides02:17

Structure and Nomenclature of Thiols and Sulfides

5.4K
Thiols and sulfides are sulfur analogs of alcohols and ethers, respectively, where the sulfur atom takes the place of the oxygen atom. Thus, thiols are generally represented as RSH, where R is an alkyl substituent and —SH is the functional group. On the other hand, in sulfides, the central sulfur atom is bonded to two hydrocarbon groups on either side. Depending upon the type of group, sulfides can be either symmetrical or asymmetrical. Both thiols and sulfides display a bent geometry,...
5.4K
Preparation and Reactions of Sulfides02:26

Preparation and Reactions of Sulfides

5.4K
Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.
5.4K
Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

7.1K
Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.
7.1K
Acetals and Thioacetals as Protecting Groups for Aldehydes and Ketones01:24

Acetals and Thioacetals as Protecting Groups for Aldehydes and Ketones

5.2K
Acetals are formed by reacting two equivalents of alcohol with carbonyl compounds like aldehydes or ketones. Acetals are unaffected by bases, nucleophiles, oxidizing agents, and reducing agents. They serve as protecting groups for aldehydes and ketones. Acetals can be easily formed and also easily removed via mild acid hydrolysis.
In the presence of multiple functional groups, when selective reduction of one group over the other is desired, groups like aldehydes and ketones that form acetals...
5.2K
Protecting Groups for Aldehydes and Ketones: Introduction01:23

Protecting Groups for Aldehydes and Ketones: Introduction

8.3K
Protecting groups are compounds that can bind to a specific functional group in the presence of other functional groups to protect them from undesired chemical reactions. These compounds can selectively bind to particular functional groups and advance chemoselective reactions in polyfunctional systems (Figure 1). After the functional group has served its purpose, it is removed by reacting it with specific compounds.
8.3K
Sulfur Assimilation01:20

Sulfur Assimilation

191
Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to...
191

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Antibiotic Resistance: From the Bench to Patients, 2.0.

Antibiotics (Basel, Switzerland)·2026
Same author

Quality by Design-Endorsed Nilotinib-Laden Liposomal Gel for Enhanced Dermal Delivery in Melanoma Management: Fabrication, Optimization, <i>In Silico, In Vitro</i>, and <i>Ex Vivo</i> Studies.

ACS applied bio materials·2026
Same author

Rapid treatment of textile wastewater using a Phragmites-derived biochar-amended hybrid constructed wetland.

Chemosphere·2026
Same author

Artemisinin and quercetin attenuate hydrogen peroxide-induced oxi-inflammatory-mitochondrial dysfunction-SASP axis mediated lung epithelial cell premature senescence via targeting Stat-1/Atm-p53/p16/p21/Bcl2, NOD-1/MAPKs/NF-κB/ signalling cascades.

Tissue & cell·2026
Same author

The HDAC Inhibitor RM-3-22 Suppresses Triple-Negative Breast Cancer by Uncoupling Autophagy to Drive FSP1-Dependent Ferroptosis.

Translational research : the journal of laboratory and clinical medicine·2026
Same author

Attitude of trainees toward tribal entrepreneurship training on solar lantern development in Ladakh: a descriptive study.

Frontiers in sociology·2026
Same journal

Electrochemical Dearomative <i>ipso</i>-Cyclization of Indolyl-ynones: A Direct Access to Trifluoromethyl/Selenyl-Spirooxindoles.

Organic letters·2026
Same journal

Photoinduced Radical Epoxidation of <i>N</i>-Alkoxyphthalimides with Allylic Peroxides.

Organic letters·2026
Same journal

B(C<sub>6</sub>F<sub>5</sub>)<sub>3</sub>-Catalyzed Ring-Opening Reaction of Bicyclo[1.1.0]butanes with Silyl Ketene Imines.

Organic letters·2026
Same journal

<i>N</i>-Sulfonylaminophthalimide-Catalyzed Aerobic Oxidative Cleavage of α-C(sp<sup>3</sup>)-H and β,γ-C(sp<sup>3</sup>)-C(sp<sup>3</sup>) Bonds of Tertiary Amines.

Organic letters·2026
Same journal

<i>O</i>-Alkylisourea-Enabled Nickel/Photoredox-Catalyzed Giese Reaction.

Organic letters·2026
Same journal

Direct Assembly of Angular 5-5-5 Tricyclic Skeletons via a Rh(III)-Catalyzed C-H Activation/Annulation Cascade.

Organic letters·2026
See all related articles

Related Experiment Video

Updated: Nov 29, 2025

Synthesis and Structure Determination of &#181;-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

13.0K

Disulfide-Based Protecting Groups for the Cysteine Side Chain.

Amit Chakraborty1, Anamika Sharma1,2, Fernando Albericio1,3,4

  • 1Peptide Science Laboratory, School of Chemistry and Physics, University of KwaZulu-Natal, Durban 4001, South Africa.

Organic Letters
|November 24, 2020
PubMed
Summary
This summary is machine-generated.

New disulfide protecting groups, SIT and MOT, simplify Cys thiol protection in solid-phase peptide synthesis (SPPS). These groups offer easy removal, overcoming challenges with existing methods like S-tert-butyl.

More Related Videos

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

6.9K
Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

10.5K

Related Experiment Videos

Last Updated: Nov 29, 2025

Synthesis and Structure Determination of &#181;-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

13.0K
Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

6.9K
Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

10.5K

Area of Science:

  • Organic Chemistry
  • Peptide Chemistry
  • Synthetic Chemistry

Background:

  • Cysteine (Cys) thiol protection is crucial in peptide synthesis.
  • Existing protecting groups like S-tert-butyl (StBu) can be difficult to remove.
  • Need for efficient and labile protecting groups in Fmoc/tBu Solid-Phase Peptide Synthesis (SPPS).

Purpose of the Study:

  • To introduce two novel disulfide-based protecting groups, SIT and MOT, for Cys thiol.
  • To provide an alternative to StBu with improved lability and stability.
  • To ensure compatibility with standard Fmoc/tBu SPPS protocols.

Main Methods:

  • Design and synthesis of novel disulfide-based protecting groups (SIT and MOT).
  • Incorporation of these groups into peptide chains using Fmoc/tBu SPPS.
  • Assessment of protecting group stability during synthesis and ease of removal post-synthesis.

Main Results:

  • SIT and MOT groups are based on secondary thiols with a β-branched point.
  • These groups exhibit efficient modulation of lability and stability.
  • Full compatibility with Fmoc/tBu SPPS was demonstrated.
  • Straightforward removal using dithiothreitol (DTT) and water was achieved.

Conclusions:

  • SIT and MOT represent effective disulfide-based protecting groups for Cys thiols.
  • They offer a significant advantage in terms of ease of removal compared to StBu.
  • These new groups are valuable tools for modern peptide synthesis.