Snorkel JK LHD
  • Snorkel JK LHD

Snorkel SS1066HF JK LHD

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Safari

Safari snorkeli Australijskog proizvodjača ARB, izradjeni od vrhunskih materijala. Za sve tipove off road vozila. Safari Snorkeli obezbeđuju vašem 4x4 terencu sa ogromnim unosom čistog vazduha na motor kada mu najviše treba. Snorkeli su stilzovani ali ipak praktični, proizvedeni koristeći visokokvalitetne ukrštene polietilenske spojeve oblikovane tako da formiraju izuzetno izdržljiv debeli zid sa neverovatnom snagom.

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    Third Degree PharmaCopyright © 2018 | 4x4 Opremao

    **Steroid B-1 (SB‑1): A synthetic 19‑norprogesterone progestin**

    | Feature | Description |
    |———|————-|
    | **Core structure** | 19‑norprogesterone (a “norpregnane” scaffold) with a Δ4,5 double bond and
    an α‑hydroxy group atCopyright © 2018 | 4x4 Oprema3. |
    | **Key functional groups** | • α‑Hydroxyl atCopyright © 2018 | 4x4 Oprema3 – confers strong progestational activity.

    • C17β‑substituent (e.g., a 1‑methyl‑2‑oxo‑ethane side chain) that enhances metabolic stability and oral
    bioavailability. |
    | **Receptor profile** | • High affinity for the progesterone receptor (PR).

    • Minimal activity at glucocorticoid, mineralocorticoid, or androgen receptors.
    |
    | **Pharmacokinetics** | • Orally active; rapid absorption.
    • Metabolized mainly by hepaticCopyright © 2018 | 4x4 OpremaYP3A4 to inactive metabolites.

    • Half‑life ~5–6 h, allowing once‑daily dosing.
    |

    —

    ### 2. Structural Features that Drive the Desired Activity

    | Feature | What It Does | Why It Matters for PR Activation |
    |———|————–|———————————-|
    | **Δ⁴-α,β-unsaturated ketone (enone) core** |
    Provides a Michael acceptor; the enone is essential for binding
    to the ligand‑binding pocket of PR. | The enone forms stabilizing π–π and hydrogen‑bond interactions with residues in the PR cavity.
    |
    | **Stereochemically defined 5α-hydroxy group** | Fixes the molecule’s three‑dimensional shape, ensuring optimal fit into the receptor’s pocket.
    | Proper orientation of the hydroxy allows for a key hydrogen bond (often to
    Ser933) that anchors the ligand. |
    | **Acyclic side chain with terminal methyl group** |
    Adds lipophilicity and extends the molecule into hydrophobic sub‑pockets of PR.
    | The methyl group interacts with hydrophobic residues, increasing binding affinity and specificity.

    |
    | **No additional bulky substituents or charged groups** | Maintains a simple pharmacophore that mimics natural
    steroids. | Simplifies synthesis and reduces potential off‑target interactions.
    |

    —

    ## 4. Why this Molecule is the “Best”Copyright © 2018 | 4x4 Opremahoice

    1. **High Binding Affinity** – Empirical data from crystallographic screening shows a
    low micromolar (often sub‑micromolar) Kd for PR,
    comparable to endogenous steroid hormones.

    2. **StructuralCopyright © 2018 | 4x4 Opremaomplementarity** – The molecule’s shape and
    electronic distribution fit precisely into the hydrophobic pocket of PR,
    maximizing van der Waals contacts and hydrogen bonding with key residues such as Ser 81 and Tyr 89 (illustrated in Fig.
    1).

    3. **Selectivity** – Because it closely mimics the natural ligand, off‑target binding to other nuclear receptors is minimized.

    4. **Chemical Stability & Solubility** – The chosen substituents confer
    sufficient aqueous solubility for experimental use while resisting metabolic degradation during short‑term assays.

    5. **Availability of Structural Data** –Copyright © 2018 | 4x4 Opremarystal structures
    (PDB IDs: 3G9Q, 4J6L) reveal the exact conformation of the ligand-binding pocket, enabling precise alignment
    and rationalization of interactions.

    —

    ## Fig. 1
    **Structural depiction of the progestin‑binding pocket
    in PGR (PDB 3G9Q).**
    The ligand (blue) occupies a hydrophobic cavity lined by residues such as Leu391,
    Phe408, and Tyr599. Hydrogen bonds with backbone carbonyls at Gly394 and Thr396 stabilize the ligand orientation. The figure illustrates how
    modifications to the progestin scaffold could enhance contacts within this pocket.

    —

    ###Copyright © 2018 | 4x4 Opremaonclusion

    The progesterone receptor’s ligand‑binding domain presents a highly defined hydrophobic cavity with strategically positioned
    hydrogen‑bond donors/acceptors, enabling precise
    interaction with natural or synthetic progestins.
    These structural features provide a robust platform
    for designing selective modulators that exploit the receptor’s unique binding chemistry while maintaining favorable pharmacokinetic properties.

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