Hi! - I'm Simon

I design beauty-products for the organic consumer segment, specialised in 100% natural formulations of all product types.


A Little About Me


Free Formulations

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Stephen Geist
Music Artist


Current Employment

Cosmetic Product Developer & QA Manager


My most recent endeavor, I develop the newest formulas for cosmetic products within the Organic certification of COSMOS sold under the brand-name of URTEKRAM.
I also handle Certifications (ECOCERT and Vegan) including audits.
In this position I have multiple persons working under me, which of course means I have leadership experience as well.
Per January 2020, I have gotten the local QA management responsibility, and manage a team of three employees.

Previous Experience

Product Developer & Safety Assessor


As safety assessor and product developer at Beauté Pacifique my week revolved around keeping on the cutting edge of toxicology, dermatology, cosmetic science, and raw material developments.

Among the daily assignments i handled research and evaluation of the clinical experiments of raw material suppliers to determine their validity.


I handled composition-requirements for the formulations along with the design and execution of product-efficacy experiments for newly developed products and raw materials.


Lastly I kept an eye on the regulatory affairs, particularly in the European Union.


In short, I made sure the products are as safe as they are effective.

R&D Laboratory Intern


Probably the actual start of my formulating career, a 2 month internship with the large Private Label manufacturer Persano.
During my internship with the R&D team at Persano Group, It has been my main responsibility to produce cosmetic products following the formulations created by the R&D team
and evaluate their physicochemical properties.

Once produced the products can be physically evaluated on a multitude of criteria, both internally and by the customer.

Laboratory Assistant


During my Masters I had half a year as a laboratory assistant at the University of Copenhagen, working amongst other things with CLP compliance.


Formal Education

Post-Graduate University Courses

Vrije Universiteit Brussel

  • 2018
  • Safety Assessment of Cosmetics in The European Union
  • 2017
  • Dermatocosmetic Science

Master of Science in Medicinal Chemistry

University of Copenhagen, Degree Awarded June 2016

Master Thesis:

Solid-phase Synthesis of Formyl Peptide Receptor 2 Ligands: On-resin Formylation and Upscaling of Peptidomimetics

Bachelor of Science in Chemistry

University of Copenhagen, Degree Awarded June 2014

Bachelor Thesis:

Solid Phase Synthesis of Solonamide B Analogues and Human Cathelicidin



Studies on acid stability and solid-phase block synthesis of peptide–peptoid hybrids: ligands for formyl peptide receptors

Anna Mette Hansen, Sarah Line Skovbakke, Simon Bendt Christensen, Iris Perez-Gassol, Henrik Franzyk

Amino Acids, 2019, 51(2):205–218

α-Peptoids as well as peptide/α-peptoid hybrids and peptide/β-peptoid hybrids constitute major classes of proteolytically stable peptidomimetics that have been extensively investigated as mimetics of biologically active peptides. Representatives of lipidated peptide/β-peptoid hybrids have been identified as promising immunomodulatory lead compounds, and hence access to these via protocols suitable for gram-scale synthesis is warranted to enable animal in vivo studies. Recent observations indicated that several byproducts appear in crude mixtures of relatively short benzyl-based peptide/β-peptoid oligomers, and that these were most predominant when the β-peptoid units displayed an α-chiral benzyl side chain. This prompted an investigation of their stability under acidic conditions. Simultaneous deprotection and cleavage of peptidomimetics containing either α-chiral α- or β-peptoid residues required treatment with strong acid only for a short time to minimize the formation of partially debenzylated byproducts. The initial work on peptide/β-peptoid oligomers with an alternating design established that it was beneficial to form the amide bond between the carboxyl group of the α-amino acid and the congested amino functionality of the β-peptoid residue in solution. To further simplify oligomer assembly on solid phase, we now present a protocol for purification-free solid-phase synthesis of tetrameric building blocks. Next, syntheses of peptidomimetic ligands via manual solid-phase methodologies involving tetrameric building blocks were found to give more readily purified products as compared to those obtained with dimeric building blocks. Moreover, the tetrameric building blocks could be utilized in automated synthesis with microwave-assisted heating, albeit the purity of the crude products was not increased.

Lactam hybrid analogues of solonamide B and autoinducing peptides as potent S. aureus AgrC antagonists

Anna Mette Hansen, Pai Peng, Mara Baldry, Iris Perez-Gassol, Simon B.Christensen, Joachim Møllesøe Obel Vinther, Hanne Ingmer, Henrik, Franzyk

European Journal of Medicinal Chemistry, 2018, 152:370-376

Emergence of antibiotic-resistant bacteria constitutes an increasing threat to human health. For example, treatment options for Staphylococcus aureus infections is declining with the worldwide spreading of highly virulent community-associated methicillin-resistant S. aureus (CA-MRSA) strains. Anti-virulence therapy has been proposed as an alternative treatment strategy, as it typically involves inhibition of expression of virulence factors rather than direct bacterial killing, thereby attenuating the risk of resistance development. An intriguing target is the agr quorum-sensing system, which is a major inducer of virulence in CA-MRSA upon activation by agr-encoded staphylococcal autoinducing peptides (AIPs).

In the present work a previously identified lactam hybrid analogue based on the marine depsipeptide solonamide B and the general structure of AIPs was investigated with respect to structure–function relationships. An array of 27 analogues exploring expansion of ring size, type of side chain, amino acid substitutions, and stereochemistry was designed and tested for AgrC-inhibitory activity. Interestingly, it was found that an analogue derived from the mirror image of the original hit proved to be the hitherto most efficient AgrC inhibitor resembling solonamide B in amino acid sequence. This and closely related compounds were 20- to 40-fold more potent in AgrC inhibition than the starting hit compound.

On‐resin N‐formylation of peptides: a head‐to‐head comparison of reagents in solid‐phase synthesis of ligands for formyl peptide receptors

Simon Bendt Christensen, Anna Mette Hansen, Henrik Franzyk

Peptide Science, 2017, 23(5):410-415

General conditions for efficient on‐resin N‐formylation of peptides were identified by screening of a number of reagents comprising aliphatic formates (ethyl formate, 2,2,2‐trifluoroethyl formate, and cyanomethyl formate), aromatic esters (phenyl formate and p‐nitrophenyl formate), and N‐formylimidazole and in situ activation of formic acid with the coupling reagent 1‐ethyl‐3‐(3‐dimethylaminopropyl)carbodiimide. Initially, reaction time and influence of solvent were examined for the formylation of a short model peptide. The most efficient reagents were examined further by using different linkers and solid supports in the synthesis of an array of longer formyl peptide ligands. For p‐nitrophenyl formate and N‐formylimidazole, almost complete conversion was reached within 2 h, albeit longer peptides attached to Tentagel resins via different linkers required an extended reaction time. Overall, the commercially available activated ester p‐nitrophenyl formate proved to be most convenient and versatile as high formylation degrees were obtained after 1–3 h at room temperature, while either conventional or microwave‐assisted heating allowed reduction of the formylation time to 20 min.

The agr Inhibitors Solonamide B and Analogues Alter Immune Responses to Staphylococccus aureus but Do Not Exhibit Adverse Effects on Immune Cell Functions

Mara Baldry, Betül Kitir, Hanne Frøkiær, Simon B. Christensen, Nico Taverne, Marjolein Meijerink, Henrik Franzyk, Christian A. Olsen, Jerry M. Wells & Hanne Ingmer

PLoS One, 2016, 11(1): e0145618.

Staphylococcus aureus infections are becoming increasingly difficult to treat due to antibiotic resistance with the community-associated methicillin-resistant S. aureus (CA-MRSA) strains such as USA300 being of particular concern. The inhibition of bacterial virulence has been proposed as an alternative approach to treat multi-drug resistant pathogens. One interesting anti-virulence target is the agr quorum-sensing system, which regulates virulence of CA-MRSA in response to agr-encoded autoinducing peptides. Agr regulation confines exotoxin production to the stationary growth phase with concomitant repression of surface-expressed adhesins. Solonamide B, a non-ribosomal depsipeptide of marine bacterial origin, was recently identified as a putative anti-virulence compound that markedly reduced expression of α-hemolysin and phenol-soluble modulins. To further strengthen solonamide anti-virulence candidacy, we report the chemical synthesis of solonamide analogues, investigation of structure–function relationships, and assessment of their potential to modulate immune cell functions. We found that structural differences between solonamide analogues confer significant differences in interference with agr, while immune cell activity and integrity is generally not affected. Furthermore, treatment of S. aureus with selected solonamides was found to only marginally influence the interaction with fibronectin and biofilm formation, thus addressing the concern that application of compounds inducing an agr-negative state may have adverse interactions with host factors in favor of host colonization.